The Protein Journal最新文献_第4页

Identification of Alternatively Spliced Novel Isoforms of Human HSPB8 Gene 人类 HSPB8 基因替代剪接新异构体的鉴定

IF 1.9 4区生物学

The Protein Journal Pub Date : 2024-07-09 DOI: 10.1007/s10930-024-10215-y

Naira Rashid, Pallavi Juneja, Akshat Rathi, Insha Sultan, Sayeed ur Rehman

{"title":"Identification of Alternatively Spliced Novel Isoforms of Human HSPB8 Gene","authors":"Naira Rashid, Pallavi Juneja, Akshat Rathi, Insha Sultan, Sayeed ur Rehman","doi":"10.1007/s10930-024-10215-y","DOIUrl":"10.1007/s10930-024-10215-y","url":null,"abstract":"<div><p>HSPB8 is a heat shock protein belonging to a family of ATP-independent stress proteins called HSPB which are present far and wide in the cells of various organisms. They are committed to protein quality control (PQC) and strive to avert protein aggregation and to procreate a pool of non-native proteins that can be swiftly folded. Their fundamental expression or stress inducibility is regulated by various cis-elements localized in the HSPB regulatory regions. In the current study we have predicted and confirmed two alternatively spliced novel transcripts of HSPB8 gene in liver, brain, and heart. These spliced variants have smaller sizes owing to smaller <i>N</i> terminal regions and showed remarkable changes in their cellular localization. Novel isoform (HSPB8-N1) was predicted to be majorly localized to nuclear region while the reported isoform (HSPB8) and one of the novel isoforms (HSPB8-N2) were predicted to be cytoplasmic in nature. There were many changes observed in the phosphorylation sites of the novel isoforms as well. The newly reported isoforms lack several structural motifs that are essential for various functional endeavors of the HSPB8 protein. In silico analysis of the conceptually translated protein was carried out using various bioinformatics tools to gain an understanding of their properties in order to explore their possible potential in therapeutics.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"43 4","pages":"782 - 792"},"PeriodicalIF":1.9,"publicationDate":"2024-07-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141560707","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Recent Advancements in Biosensors for the Detection and Characterization of Amyloids: A Review 用于检测和表征淀粉样蛋白的生物传感器的最新进展：综述。

IF 1.9 4区生物学

The Protein Journal Pub Date : 2024-06-02 DOI: 10.1007/s10930-024-10205-0

Md Harun Rashid, Priyankar sen

{"title":"Recent Advancements in Biosensors for the Detection and Characterization of Amyloids: A Review","authors":"Md Harun Rashid, Priyankar sen","doi":"10.1007/s10930-024-10205-0","DOIUrl":"10.1007/s10930-024-10205-0","url":null,"abstract":"<div><p>Modern medicine has increased the human lifespan. However, with an increase in average lifespan risk of amyloidosis increases. Amyloidosis is a condition characterized by protein misfolding and aggregation. Early detection of amyloidosis is crucial, yet conventional diagnostic methods are costly and lack precision, necessitating innovative tools. This review explores recent advancements in diverse amyloid detection methodologies, highlighting the need for interdisciplinary research to develop a miniaturized electrochemical biosensor leveraging nanotechnology. However, the diagnostics industry faces obstacles such as skilled labor shortages, standardized selection processes, and concurrent multi-analyte identification challenges. Research efforts are focused on integrating electrochemical techniques into clinical applications and diagnostics, with the successful transition of miniaturized technologies from development to testing posing a significant hurdle. Label-free transduction techniques like voltammetry and electrochemical impedance spectroscopy (EIS) have gained traction due to their rapid, cost-effective, and user-friendly nature.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"43 4","pages":"656 - 674"},"PeriodicalIF":1.9,"publicationDate":"2024-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141187230","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Bioinformatics Analysis of Actin Interactome: Characterization of the Nuclear and Cytoplasmic Actin-Binding Proteins 肌动蛋白相互作用组的生物信息学分析：核与细胞质肌动蛋白结合蛋白的特征描述

IF 1.9 4区生物学

The Protein Journal Pub Date : 2024-06-02 DOI: 10.1007/s10930-024-10207-y

Yakov I. Mokin, Olga I. Povarova, Iuliia A. Antifeeva, Alexey V. Artemov, Vladimir N. Uversky, Konstantin K. Turoverov, Irina M. Kuznetsova, Alexander V. Fonin

{"title":"Bioinformatics Analysis of Actin Interactome: Characterization of the Nuclear and Cytoplasmic Actin-Binding Proteins","authors":"Yakov I. Mokin, Olga I. Povarova, Iuliia A. Antifeeva, Alexey V. Artemov, Vladimir N. Uversky, Konstantin K. Turoverov, Irina M. Kuznetsova, Alexander V. Fonin","doi":"10.1007/s10930-024-10207-y","DOIUrl":"10.1007/s10930-024-10207-y","url":null,"abstract":"<div><p>Actin is present in the cytoplasm and nucleus of every eukaryotic cell. In the cytoplasm, framework and motor functions of actin are associated with its ability to polymerize to form F-actin. In the nucleus, globular actin plays a significant functional role. For a globular protein, actin has a uniquely large number of proteins with which it interacts. Bioinformatics analysis of the actin interactome showed that only a part of actin-binding proteins are both cytoplasmic and nuclear. There are proteins that interact only with cytoplasmic, or only with nuclear actin. The first pool includes proteins associated with the formation, regulation, and functioning of the actin cytoskeleton predominate, while nuclear actin-binding proteins are involved in the majority of key nuclear processes, from regulation of transcription to DNA damage response. Bioinformatics analysis of the structure of actin-binding proteins showed that these are mainly intrinsically disordered proteins, many of which are part of membrane-less organelles. Interestingly, although the number of intrinsically disordered actin-binding proteins in the nucleus is greater than in the cytoplasm, the drivers for the formation of the membrane-less organelles in the cytoplasm are significantly (four times) greater than in the nucleus.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"43 4","pages":"675 - 682"},"PeriodicalIF":1.9,"publicationDate":"2024-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141187225","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Exploring the Potential of Arginine to Increase Coelenterazine-Renilla Luciferase Affinity and Enzyme Stability: Kinetic and Molecular Dynamics Studies 探索精氨酸提高腔肠素-瑞尼拉荧光素酶亲和力和酶稳定性的潜力：动力学和分子动力学研究。

IF 1.9 4区生物学

The Protein Journal Pub Date : 2024-06-02 DOI: 10.1007/s10930-024-10208-x

Maryam Salehian, Rahman Emamzadeh, Mahboobeh Nazari

{"title":"Exploring the Potential of Arginine to Increase Coelenterazine-Renilla Luciferase Affinity and Enzyme Stability: Kinetic and Molecular Dynamics Studies","authors":"Maryam Salehian, Rahman Emamzadeh, Mahboobeh Nazari","doi":"10.1007/s10930-024-10208-x","DOIUrl":"10.1007/s10930-024-10208-x","url":null,"abstract":"<div><p><i>Renilla</i> luciferase catalyzes the oxidation of coelenterazine to coelenteramide and results in the emission of a photon of light. Although <i>Renilla</i> luciferase has various applications in biotechnology, its low thermal stability limits the development of its applications. Arginine is a well-known stabilizing amino acid that plays a key role in protein stabilization against inactivation. However, its impact on enzyme properties is unpredictable. This study investigates the impact of arginine on the kinetics and thermal stability of <i>Renilla</i> luciferase. The enzyme's performance was significantly enhanced in the presence of arginine, with catalytic efficiency increasing by 3.31-fold and 3.08-fold when exposed to 0.2 M and 0.3 M arginine, respectively. Additionally, arginine improved the thermal stability of <i>Renilla</i> luciferase. Molecular dynamics simulation showed that the addition of 0.2 M arginine reduced the binding of coelenteramide, the reaction product and an enzyme inhibitor, to the active site of the <i>Renilla</i> luciferase. Therefore, the release of the product was accelerated, and the affinity of <i>Renilla</i> luciferase for coelenterazine increased. Furthermore, Molecular dynamics studies indicated an increased network of water molecules surrounding <i>Renilla</i> luciferase in the presence of 0.2 M arginine. This network potentially enhances the hydrophobic effect on the protein structure, ultimately improving enzyme stability. The findings of this study hold promise for the development of commercial kits incorporating <i>Renilla</i> luciferase.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"43 4","pages":"739 - 750"},"PeriodicalIF":1.9,"publicationDate":"2024-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141187227","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Molecular Insights of an Avian Species with Low Oxygen Affinity, the Crystal Structure of Duck T-State Methemoglobin 对低氧亲和力禽类物种的分子认识--鸭 T 态高铁血红蛋白的晶体结构。

IF 1.9 4区生物学

The Protein Journal Pub Date : 2024-05-20 DOI: 10.1007/s10930-024-10206-z

Sathya Moorthy Ponnuraj, Neelagandan Kamariah, Balasubramanian Moovarkumudalvan, Ramya Ramadoss, M. N. Ponnuswamy

{"title":"Molecular Insights of an Avian Species with Low Oxygen Affinity, the Crystal Structure of Duck T-State Methemoglobin","authors":"Sathya Moorthy Ponnuraj, Neelagandan Kamariah, Balasubramanian Moovarkumudalvan, Ramya Ramadoss, M. N. Ponnuswamy","doi":"10.1007/s10930-024-10206-z","DOIUrl":"10.1007/s10930-024-10206-z","url":null,"abstract":"<div><p>Hemoglobin (Hb) is the key metalloprotein within red blood cells involved in oxygen transportation from lungs to body cells. The heme-iron atom inherent within Hb effectuates the mechanism of oxygen transportation and carbon dioxide removal. Structural investigations on avian Hb are limited when compared with the enormous work has been carried out on mammalian Hb. Here, the crystal structure of T-state methemoglobin (T-metHb) from domestic duck (<i>Anas platyrhynchos</i>), a low oxygen affinity avian species, determined to 2.1Å resolution is presented. Duck T-metHb crystallized in the orthorhombic space group C222<sub>1</sub> with unit cell parameters a = 59.89, b = 109.42 and c = 92.07Å. The final refined model with R-factor: 19.5% and R<sub>free</sub>: 25.2% was obtained. The structural analysis reveals that duck T-metHb adopts a unique quaternary structure that is distinct from any of the avian liganded Hb structures. Moreover, it closely resembles the deoxy Hb of bar-headed goose, a high oxygen-affinity species. Besides the amino acid αPro119 located in the α1β1 interface, a unique quaternary structure with a constrained heme environment is attributed for the intrinsic low oxygen-affinity of duck Hb. This study reports the first protein crystal structure of low oxygen-affinity avian T-metHb from <i>Anas platyrhynchos</i>.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"43 4","pages":"771 - 781"},"PeriodicalIF":1.9,"publicationDate":"2024-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141066347","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Expression of Recombinant Stonustoxin Alpha Subunit and Preparation of polyclonal antiserum for Stonustoxin Neutralization Studies 重组石蒜毒素α亚基的表达和用于石蒜毒素中和研究的多克隆抗血清的制备。

IF 1.9 4区生物学

The Protein Journal Pub Date : 2024-05-17 DOI: 10.1007/s10930-024-10203-2

Amir Sajjad Hojjati-Razgi, Shahram Nazarian, Hossein Samiei-Abianeh, Amir Vazirizadeh, Emad kordbacheh, Seyed Mojtaba Aghaie

{"title":"Expression of Recombinant Stonustoxin Alpha Subunit and Preparation of polyclonal antiserum for Stonustoxin Neutralization Studies","authors":"Amir Sajjad Hojjati-Razgi, Shahram Nazarian, Hossein Samiei-Abianeh, Amir Vazirizadeh, Emad kordbacheh, Seyed Mojtaba Aghaie","doi":"10.1007/s10930-024-10203-2","DOIUrl":"10.1007/s10930-024-10203-2","url":null,"abstract":"<div><p>Stonustoxin (SNTX) is a lethal protein found in stonefish venom, responsible for many of the symptoms associated with stonefish envenomation. To counter stonefish venom challenges, antivenom is a well-established and effective solution. In this study, we aimed to produce the recombinant alpha subunit protein of Stonustoxin from <i>Synanceia horrida</i> and prepare antibodies against it The SNTXα gene sequence was optimized for <i>E. coli</i> BL21 (DE3) expression and cloned into the pET17b vector. Following purification, the recombinant protein was subcutaneously injected into rabbits, and antibodies were extracted from rabbit´s serum using a G protein column As a result of codon optimization, the codon adaptation index for the SNTXα cassette increased to 0.94. SDS-PAGE analysis validated the expression of SNTXα, with a band observed at 73.5 kDa with a yield of 60 mg/l. ELISA results demonstrated rabbits antibody titers were detectable up to a 1:256,000 dilution. The isolated antibody from rabbit´s serum exhibited a concentration of 1.5 mg/ml, and its sensitivity allowed the detection of a minimum protein concentration of 9.7 ng. In the neutralization assay the purified antibody against SNTXα protected mice challenged with 2 LD50. In conclusion, our study successfully expressed the alpha subunit of Stonustoxin in a prokaryotic host, enabling the production of antibodies for potential use in developing stonefish antivenom.</p><h3>Graphical Abstract</h3>\u0000<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"43 3","pages":"627 - 638"},"PeriodicalIF":1.9,"publicationDate":"2024-05-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140963370","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Molecular Cloning, Expression and Enzymatic Characterization of Tetrahymena thermophila Glutathione-S-Transferase Mu 34 嗜热四膜虫谷胱甘肽-S-转移酶 Mu 34 的分子克隆、表达和酶学特征。

IF 1.9 4区生物学

The Protein Journal Pub Date : 2024-05-14 DOI: 10.1007/s10930-024-10204-1

Handan Açelya Kapkaç, Muhittin Arslanyolu

{"title":"Molecular Cloning, Expression and Enzymatic Characterization of Tetrahymena thermophila Glutathione-S-Transferase Mu 34","authors":"Handan Açelya Kapkaç, Muhittin Arslanyolu","doi":"10.1007/s10930-024-10204-1","DOIUrl":"10.1007/s10930-024-10204-1","url":null,"abstract":"<div><p>Glutathione-S-transferase enzymes (GSTs) are essential components of the phase II detoxification system and protect organisms from oxidative stress induced by xenobiotics and harmful toxins such as 1-chloro-2,4-dinitrobenzene (CDNB). In <i>Tetrahymena thermophila</i>, the TtGSTm34 gene was previously reported to be one of the most responsive GST genes to CDNB treatment (LD50 = 0.079 mM). This study aimed to determine the kinetic features of recombinantly expressed and purified TtGSTm34 with CDNB and glutathione (GSH). TtGSTm34-8xHis was recombinantly produced in <i>T. thermophila</i> as a 25-kDa protein after the cloning of the 660-bp full-length ORF of TtGSTm34 into the pIGF-1 vector. A three-dimensional model of the TtGSTm34 protein constructed by the AlphaFold and PyMOL programs confirmed that it has structurally conserved and folded GST domains. The recombinant production of TtGSTm34-8xHis was confirmed by SDS‒PAGE and Western blot analysis. A dual-affinity chromatography strategy helped to purify TtGSTm34-8xHis approximately 3166-fold. The purified recombinant TtGSTm34-8xHis exhibited significantly high enzyme activity with CDNB (190 µmol/min/mg) as substrate. Enzyme kinetic analysis revealed <i>K</i><sub>m</sub> values of 0.68 mM with GSH and 0.40 mM with CDNB as substrates, confirming its expected high affinity for CDNB. The optimum pH and temperature were determined to be 7.0 and 25 °C, respectively. Ethacrynic acid inhibited fully TtGSTm34-8xHis enzyme activity. These results imply that TtGSTm34 of <i>T. thermophila</i> plays a major role in the detoxification of xenobiotics, such as CDNB, as a first line of defense in aquatic protists against oxidative damage.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"43 3","pages":"613 - 626"},"PeriodicalIF":1.9,"publicationDate":"2024-05-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140924242","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Expression, Purification and Characterization of Recombinant Disintegrin from Gloydius Brevicaudus Venom in Escherichia Coli 在大肠杆菌中表达、纯化和表征来自 Gloydius Brevicaudus 毒液的重组崩解素。

IF 1.9 4区生物学

The Protein Journal Pub Date : 2024-05-11 DOI: 10.1007/s10930-024-10198-w

Yinxiang Lan, Xiuliang Qiu, Yunlu Xu

{"title":"Expression, Purification and Characterization of Recombinant Disintegrin from Gloydius Brevicaudus Venom in Escherichia Coli","authors":"Yinxiang Lan, Xiuliang Qiu, Yunlu Xu","doi":"10.1007/s10930-024-10198-w","DOIUrl":"10.1007/s10930-024-10198-w","url":null,"abstract":"<div><p>Disintegrins, a family of snake venom protein, which are capable of modulating the activity of integrins that play a fundamental role in the regulation of many physiological and pathological processes. The main purpose of this study is to obtain the recombinant disintegrin (r-DI) and evaluate its biological activity. In this study, we explored a high-level expression prokaryotic system and purification strategy for r-DI. Then, r-DI was treated to assay effects on cell growth, migration, and invasion. The affinity for the interactions of r-DI with integrin was determined using Surface plasmon resonance (SPR) analyses. The r-DI can be expressed in <i>Escherichia coli</i> and purified by one-step chromatography. The r-DI can inhibit B16F10 cells proliferation, migration, and invasion. Also, we found that r-DI could interact with the integrin <b>αIIbβ3</b> (GPIIb/IIIa). The r-DI can be expressed, purified, characterized through functional assays, and can also maintain strong biological activities. Thus, this study showed potential therapeutic effects of r-DI for further functional and structural studies.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"43 3","pages":"603 - 612"},"PeriodicalIF":1.9,"publicationDate":"2024-05-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140909674","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The Impact of Terminal Peptide Extensions of Retinal Inosine 5´Monophosphate Dehydrogenase 1 Isoforms on their DNA-binding Activities 视网膜肌苷-5´单磷酸脱氢酶 1 异构体的末端肽延伸对其 DNA 结合活性的影响

IF 1.9 4区生物学

The Protein Journal Pub Date : 2024-05-11 DOI: 10.1007/s10930-024-10202-3

Mohsen Nabi Afjadi, Razieh Yazdanparast, Ebrahim Barzegari

{"title":"The Impact of Terminal Peptide Extensions of Retinal Inosine 5´Monophosphate Dehydrogenase 1 Isoforms on their DNA-binding Activities","authors":"Mohsen Nabi Afjadi, Razieh Yazdanparast, Ebrahim Barzegari","doi":"10.1007/s10930-024-10202-3","DOIUrl":"10.1007/s10930-024-10202-3","url":null,"abstract":"<div><p>The main structural difference between the mutation-susceptible retinal isoforms of inosine 5´-monophosphate dehydrogenase-1 (IMPDH-1) with the canonical form resides in the C- and N-terminal peptide extensions with unknown structural/functional impacts. In this report, we aimed to experimentally evaluate the functional impact of these extensions on the specific/non-specific single-stranded DNA (ssDNA)-binding activities relative to those of the canonical form. Our in silico findings indicated the possible contribution of the C-terminal segment to the reduced flexibility of the Bateman domain of the enzyme. In addition, the in silico data indicated that the N-terminal tail acts by altering the distance between the tetramers in the concave octamer complex (the native form) of the enzyme. The overall impact of these predicted structural variations became evident, first, through higher K<sub>m</sub> values with respect to either of the substrates relative to the canonical isoform, as reported previously (Andashti et al. in Mol Cell Biochem 465(1):155-164, 2020). Secondary, the binding of the recombinant mouse retinal isoform IMPDH1 (603) to its specific Rhodopsin target gene was significantly augmented while its binding to non-specific ssDNA was lower than that of the canonical isoform. The DNA-binding activity of the other mouse retinal isoform, IMPDH1(546), to specific and non-specific ssDNA was lower than that of the canonical form most probably due to the in silico predicted rigidity created in the Bateman domain by the C-terminal peptide extension. Furthermore, the DNA binding to the Rhodopsin target gene by each of the IMPDH isoforms influenced in the presence of GTP (Guanosine triphosphate) and ATP (Adenosine triphosphate).</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"43 3","pages":"592 - 602"},"PeriodicalIF":1.9,"publicationDate":"2024-05-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140909675","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Understanding the Specific Implications of Amino Acids in the Antibody Development 了解氨基酸在抗体发展中的具体影响。

IF 1.9 4区生物学

The Protein Journal Pub Date : 2024-05-09 DOI: 10.1007/s10930-024-10201-4

Akshata Gavade, Anil Kumar Nagraj, Riya Patel, Roylan Pais, Pratiksha Dhanure, Juergen Scheele, Werner Seiz, Jaspal Patil

{"title":"Understanding the Specific Implications of Amino Acids in the Antibody Development","authors":"Akshata Gavade, Anil Kumar Nagraj, Riya Patel, Roylan Pais, Pratiksha Dhanure, Juergen Scheele, Werner Seiz, Jaspal Patil","doi":"10.1007/s10930-024-10201-4","DOIUrl":"10.1007/s10930-024-10201-4","url":null,"abstract":"<div><p>As the demand for immunotherapy to treat and manage cancers, infectious diseases and other disorders grows, a comprehensive understanding of amino acids and their intricate role in antibody engineering has become a prime requirement. Naturally produced antibodies may not have the most suitable amino acids at the complementarity determining regions (CDR) and framework regions, for therapeutic purposes. Therefore, to enhance the binding affinity and therapeutic properties of an antibody, the specific impact of certain amino acids on the antibody’s architecture must be thoroughly studied. In antibody engineering, it is crucial to identify the key amino acid residues that significantly contribute to improving antibody properties. Therapeutic antibodies with higher binding affinity and improved functionality can be achieved through modifications or substitutions with highly suitable amino acid residues. Here, we have indicated the frequency of amino acids and their association with the binding free energy in CDRs. The review also analyzes the experimental outcome of two studies that reveal the frequency of amino acids in CDRs and provides their significant correlation between the outcomes. Additionally, it discusses the various bond interactions within the antibody structure and antigen binding. A detailed understanding of these amino acid properties should assist in the analysis of antibody sequences and structures needed for designing and enhancing the overall performance of therapeutic antibodies.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"43 3","pages":"405 - 424"},"PeriodicalIF":1.9,"publicationDate":"2024-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140900562","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0