Biochimica et biophysica acta. Proteins and proteomics最新文献

{"title":"Structural-functional relevance of DNAJBs in protein aggregation and associated neurodegenerative diseases","authors":"Siraj Fatima ,&nbsp;Priyanka Pandey ,&nbsp;Sandeep K. Sharma ,&nbsp;Smriti Priya","doi":"10.1016/j.bbapap.2025.141074","DOIUrl":"10.1016/j.bbapap.2025.141074","url":null,"abstract":"<div><div>DNAJ proteins, also known as HSP40s, are co-chaperones that regulate the multifunctionality of HSP70s in maintaining cellular protein homeostasis. The heterogeneous family of DNAJ co-chaperones is classified into three classes (A, B and C), where structural diversity within the class defines their specific functions. Among three classes, the DNAJB class of co-chaperones are associated with cellular compartment-specific protein folding, disaggregation and degradation of proteins and enables effective targeting of a broad spectrum of aggregation-prone substrate proteins. The structural divergence of DNAJBs is critical for regulating disaggregation and degradation functions through specific interactions with HSP70 and substrate proteins. While the role of DNAJBs in maintaining protein homeostasis is valuable in addressing protein aggregation in neurodegenerative diseases, a limited understanding of their mechanisms and cellular functions beyond co-chaperones restricts their therapeutic applications. In this review, the mechanism of DNAJBs regulating aggregation of pathogenic proteins such as α-synuclein, tau, amyloid-β, and huntingtin are discussed. Emphasis on the selectivity of DNAJBs towards folding, disaggregation and degradation functions of HSP70, substrate selection and involvement of different structural regions are explained to provide a structural and functional understanding of DNAJB proteins. Mutations in different DNAJBs linked with several proteins aggregation-related neuronal and neuromuscular diseases are discussed. The fundamental understanding of DNAJB diversity and functionality can assist future interventions for regulating protein homeostasis and managing associated diseases.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 4","pages":"Article 141074"},"PeriodicalIF":2.5,"publicationDate":"2025-04-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143868449","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}

{"title":"Role of electrostatics in cold adaptation: A comparative study of eury- and stenopsychrophilic triose phosphate isomerase","authors":"Jan S. Nowak ,&nbsp;Sune Olesen ,&nbsp;Pengfei Tian ,&nbsp;René L. Bærentsen ,&nbsp;Ditlev E. Brodersen ,&nbsp;Daniel E. Otzen","doi":"10.1016/j.bbapap.2025.141072","DOIUrl":"10.1016/j.bbapap.2025.141072","url":null,"abstract":"<div><div>Psychrophilic (cold-active) organisms have developed enzymes that facilitate sufficient metabolic activity at low temperatures to sustain life. This occurs through molecular adaptations that tend to increase protein flexibility at the expense of stability. However, psychrophiles also vary in their growth conditions. Eurypsychrophiles thrive over a wide temperature range and often prefer temperatures above 20 °C, while stenopsychrophiles grow optimally below 15 °C and are more narrowly adapted to cold temperatures. To elucidate differences between these two classes of enzymes, we here compare the stability and unfolding kinetics of two orthologues of the basal household enzyme triose phosphate isomerase, one from the stenopsychrophilic Antarctic permafrost bacterium <em>Rhodonellum psychrophilum</em> (sTPI) and the other from the eurypsychrophilic Greenland ikaite column bacterium <em>Rhodococcus</em> sp. <em>JG-3</em> (eTPI). Remarkably, sTPI proved significantly more thermostable and resistant to chemical denaturation than its eurypsychrophilic counterpart, eTPI, in the absence of ionic components in solution, whereas inclusion of electrostatic screening agents in the form of sodium chloride or the charged denaturant guanidinium chloride largely cancelled out this difference. Thus, electrostatics play a prominent role in stabilizing the stenopsychrophilic sTPI, and a mandatory low-temperature growth environment does not preclude the development of considerable thermotolerance for individual enzymes. We were able to increase the thermostability of sTPI using an evolutionary machine learning model, which transferred several sTPI residues into the eTPI active site. While the stabilizing effect was modest, the combination of individual mutations was additive, underscoring the potential of combining multiple beneficial mutations to achieve enhanced enzyme properties.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 4","pages":"Article 141072"},"PeriodicalIF":2.5,"publicationDate":"2025-04-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143829366","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}

{"title":"Exploring human carboxylesterases 1 and 2 selectivity of two families of substrates at an atomistic level","authors":"Sergio R. Ribone ,&nbsp;Dario A. Estrin ,&nbsp;Mario A. Quevedo","doi":"10.1016/j.bbapap.2025.141069","DOIUrl":"10.1016/j.bbapap.2025.141069","url":null,"abstract":"<div><div>Human carboxylesterases (CES) are enzymes that play an important role in the metabolism and biotransformation of diverse substances. The two more relevant isoforms, CES1A1 and CES2A1, catalyze the hydrolysis of numerous approved drugs and prodrugs. The elucidation of CES isoform substrates specificity constitutes a very relevant medicinal chemistry issue. The general role pointed that the selectivity towards CES1A1 or CES2A1 depends on the size of the acyl and alkyl moieties present in the structure of the substrate, but several exceptions regarding substrate promiscuity towards both CES have been reported. In this work, a combination of classical molecular dynamics (MD) and hybrid quantum mechanics/molecular mechanics (QM/MM) simulations were applied with the purpose of studying the substrate selectivity of CES1A1 and CES2A1 on two sets of selected ligands: <em>p</em>-nitrophenyl ester derivatives (NPE) and pyrethroid stereoisomers (Pyr). The classical molecular modeling studies showed that the van der Waals (VDW) component of interaction, with the hydrophobic residues present on CES1A1 and CES2A1 subpocket 1 and subpocket 2, showed a significant contribution to the substrates-CES affinity properties. The hybrid QM/MM simulations exhibited that the rate-limiting step for the studied substrates reactions were related to the transition state (TS) with the higher steric hindrance molecular structure. In conclusion, it was possible to observe that the studied substrates generate the best possible interaction pattern with the residues from subpocket 1 and 2 in order to produce the corresponding affinity constant with the enzyme. Then, this interaction pattern drives the catalytic turn-over reaction through the presence or absence of a high steric hindrance center in the molecular structure of the rate-limiting reaction.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 4","pages":"Article 141069"},"PeriodicalIF":2.5,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143821517","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}

{"title":"Green tea polyphenol EGCG acts differentially on end-stage amyloid polymorphs of α-synuclein formed in different polyol osmolytes","authors":"Santosh Devi ,&nbsp;Dushyant K. Garg ,&nbsp;Rajiv Bhat","doi":"10.1016/j.bbapap.2025.141073","DOIUrl":"10.1016/j.bbapap.2025.141073","url":null,"abstract":"<div><div>Synucleinopathies are heterogenous group of disorders characterized by α-synuclein amyloid aggregates in the nervous system. Different synucleinopathy clinical subtypes are encoded by structurally diverse α-synuclein amyloid polymorphs referred to as ‘strains’. The underlying structural differences between polymorphs can potentially hamper the drug design against synucleinopathies. Polyphenolic compounds like EGCG have shown promise in inhibiting and remodeling of α-synuclein amyloid aggregates, but their effects on different polymorphs are not well-studied. The cellular environment is one factor contributing to the heterogeneity in the amyloid landscape. Herein, we generated diverse polymorphs of α-synuclein by fine-tuning its aggregation using different polyol osmolytes, varying in their physicochemical properties. These osmolytes act as globular protein stabilizers and conformational modulators of intrinsically disordered proteins. While the buffer control α-synuclein aggregates were evenly dispersed, the polyol-induced aggregate solutions contained a heterogeneous mixture of <em>co</em>-existing polymorphs, as evidenced by AFM and TEM measurements. The polyol-induced aggregated solutions consisted of a mixture of both fibrillar and nonfibrillar cross-β-rich species. Using various spectroscopic tools, we observed differences in the structures of osmolyte-induced polymorphic aggregates. We incubated these aggregates with EGCG and observed its disparate action over polymorphs wherein the treated species were either disintegrated or structurally altered. Contrary to previous reports, all EGCG-treated polymorphs were β-sheet-rich and seeding-competent. Our findings are relevant in assessing the efficacy of polyphenolic compounds on diverse aggregate strains encoding different proteinopathy variants. The formation of β-sheet-rich species in our study also engenders a more critical examination of EGCG's mode of action on diverse classes of amyloids.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 4","pages":"Article 141073"},"PeriodicalIF":2.5,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143794633","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}

{"title":"Crystal structure of thymidine kinase from the multi-drug resistant col strain of Staphylococcus aureus","authors":"Anam Ashraf ,&nbsp;Ravi Kant Pal ,&nbsp;Md. Imtaiyaz Hassan","doi":"10.1016/j.bbapap.2025.141071","DOIUrl":"10.1016/j.bbapap.2025.141071","url":null,"abstract":"<div><div>Thymidine kinase (TK) is a key enzyme in the salvage pathway of thymidine that produces thymidine monophosphate. TK enzyme activity is tightly coupled to the cell cycle, exhibiting marked fluctuations in expression and activity. We report the crystal structure of TK from the <em>Staphylococcus aureus col</em> strain (Sa-TK), which has emerged as a promising therapeutic target. The overall structure of Sa-TK closely resembles that of human TK. The lasso region in the structure shows an open conformation due to the absence of a natural substrate. The phosphate donor site is bound with sulfate ions from the crystallization conditions. The P-loop is visible, but the complete P-β hairpin cannot be traced due to the flexibility of this region. Sa-TK assembles as a tetramer with unique inter-subunit interactions involving salt bridges between charged residues. Glu136 and Arg184, as well as Arg154 and Glu102 from each of the subunits, have β-sheet interactions that form salt bridges. The catalytically active site residue Glu89 is conserved, which is essential for enzyme activity. Sa-TK lacks a longer C-terminal sequence involved in mitotic regulation through proteolytic degradation, a feature that is likely absent in Sa-TK. The crystal structure of Sa-TK offers detailed insights into its structural and functional properties, highlighting its conserved nature and emphasizing the challenge of developing selective inhibitors that do not affect host TK. This detailed structural information presents a valuable opportunity for the rational design of novel antibacterial agents specifically targeting Sa-TK, offering a promising avenue for combating <em>S. aureus</em> infections.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 4","pages":"Article 141071"},"PeriodicalIF":2.5,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143785301","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}

{"title":"TMB Stab-pred: Predicting the stability of transmembrane β-barrel proteins using their sequence and structural signatures","authors":"P. Ramakrishna Reddy,&nbsp;A. Kulandaisamy,&nbsp;M. Michael Gromiha","doi":"10.1016/j.bbapap.2025.141070","DOIUrl":"10.1016/j.bbapap.2025.141070","url":null,"abstract":"<div><div>Understanding the folding and stability of transmembrane β-barrel proteins (TMBs) provides insights into their structural integrity, functional mechanisms, and implications for disease states. In this work, we have characterized the important features that influence the folding and stability of TMBs. Our results showed that lipid accessible surface area and transition energy are important for understanding the stability of TMBs. Further, this information was utilized to develop a linear regression-based method for predicting the stability of TMBs. Our method achieved a correlation and mean absolute error (MAE) of 0.96 and 0.94 kcal/mol on the jack-knife test. Moreover, we compared the stability of TMBs with globular all-β proteins and observed that long-range interactions and energetic properties are crucial for maintaining the stability of both β-barrel membrane and all-β globular proteins. On the other hand, side-chain – side-chain hydrogen bonds and lipid accessible surface area are specific to membrane proteins. These features are critical for membrane proteins because they influence a protein to embed within the membrane environment. Further, we have developed a web server, TMB Stab-pred for predicting the stability of TMBs, and it is accessible at <span><span>https://web.iitm.ac.in/bioinfo2/TMBB/index.html</span><svg><path></path></svg></span>.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 4","pages":"Article 141070"},"PeriodicalIF":2.5,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143794638","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}

{"title":"Synovial fluid glycoproteome profiling in knee osteoarthritis: Molecular insights into type 2 diabetes-associated biomarkers and therapeutic targets","authors":"Monidipa Konar ,&nbsp;Bhavneet Kaur ,&nbsp;Uttam Chand Saini ,&nbsp;Sanjay K. Bhadada ,&nbsp;Sadhna Sharma","doi":"10.1016/j.bbapap.2025.141067","DOIUrl":"10.1016/j.bbapap.2025.141067","url":null,"abstract":"<div><div>Type 2 diabetes mellitus (T2DM) and Osteoarthritis (OA) share common risk factors like age, obesity and hypertension. Currently, 52 % of diabetic patients suffer from arthritis. Diabetes facilitates OA by altering lipid metabolism, levels of adipokines &amp; cytokines, accumulation of advanced glycation end products, etc., which affects cartilage &amp; bone health. However, the molecular mechanisms of the association of OA with T2DM remain unexplored. Since diabetes greatly affects the glycosylation status of proteins, the present study focused on identifying glycoproteins that could serve as diagnostic and prognostic markers for identifying osteoarthritis in diabetic individuals by LC-MS/MS. Comparative proteomic analysis revealed 20 significantly altered glycoproteins; among them, thyroxine-binding globulin (THBG), alpha-1-antitrypsin (A1AT), fibrinogen gamma chain (FGG) and angiotensinogen (AGT) were further validated. THBG, A1AT and AGT showed promising potential to identify the comorbid condition in serum and synovial fluid, however, ROC analysis identified THBG as the best candidate glycoprotein marker. Upregulation of THBG in OADM disrupts the bone remodeling cycle, degrades insulin, and promotes the expression of GLUT-1 and MMP-9. Overall, THBG could also serve as a therapeutic target for reducing the progression of osteoarthritis and alleviating pain and bone stiffness associated with the disease.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 4","pages":"Article 141067"},"PeriodicalIF":2.5,"publicationDate":"2025-03-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143742091","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}

{"title":"Efficient production of a novel recombinant fusion protein of EIEC effector IpaD and EGFP: Biophysical characterization and functional studies","authors":"Sudeshna Halder,&nbsp;Namita Jaiswal,&nbsp;Salari Charan Balajee,&nbsp;Nibedita Mahata","doi":"10.1016/j.bbapap.2025.141066","DOIUrl":"10.1016/j.bbapap.2025.141066","url":null,"abstract":"<div><div>The conserved invasion plasmid antigen D (IpaD) protein demonstrates broad protective capabilities against bacillary dysentery caused by Enteroinvasive <em>Escherichia coli</em> (EIEC) and <em>Shigella</em>. However, the instability of the IpaD protein at room temperature limits its therapeutic potential. The stabilization and efficient production of functional recombinant proteins remain critical challenges in therapeutic and vaccine development. This study presents a novel fluorescence fusion strategy for producing a stable IpaD-EGFP recombinant protein using a flexible linker (GGGGS)₃. The fusion technique enhances the expression level (∼53 %), solubility (∼77 %), and stability of the IpaD-EGFP fusion protein. Biophysical characterization studies suggest that the IpaD-EGFP fusion protein is stable at refrigerated temperatures for extended periods and up to 1 month at 25 °C. The IpaD-EGFP protein triggers apoptosis in Raw 267.4 cells through activation of caspases 3/7. The protein also induces antibody response in BALB/c mice indicating its immunogenicity. Together, these findings indicate that IpaD-EGFP generated in this study is a potential approach for the design and production of stable IpaD-based protein therapeutics, breaking the expensive “cold chain” of continuous refrigeration. Fusion approach significantly enhanced the solubility, yield, and stability of IpaD, while enabling efficient purification.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 4","pages":"Article 141066"},"PeriodicalIF":2.5,"publicationDate":"2025-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143630132","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}

{"title":"Tracking heme biology with resonance Raman spectroscopy","authors":"Amanda Bartkowiak,&nbsp;Ewa Szczesny-Malysiak,&nbsp;Jakub Dybas","doi":"10.1016/j.bbapap.2025.141065","DOIUrl":"10.1016/j.bbapap.2025.141065","url":null,"abstract":"<div><div>Heme proteins are a large group of biomolecules with heme incorporated as a prosthetic group. Apart from cytochromes present in almost all cell types, many other specific heme proteins are expressed in different kinds of cells, e.g. hemoglobin in the erythrocytes, myoglobin (skeletal and vascular smooth muscle cells), cytoglobin (fibroblasts) and neuroglobin (neurons and retina). Among their wide and diverse biological functions, the most important is their unique ability to bind, store, and transport gaseous molecules, such as oxygen, carbon monoxide, and nitric oxide. Resonance Raman (RR) spectroscopy is an exceptional analytical tool that allows for qualitative and quantitative characterization of heme proteins in biological systems. Due to its high sensitivity, even subtle structural alterations of the heme group can be monitored and tracked during cellular processes. Resonance Raman excitation within the Soret absorption band (390–440 nm) provides rich information on the environment of heme's active site, allowing differentiation of the iron ion oxidation and spin states, and tracking the movement of the porphyrin ring plane in response to the changes in oxygenation status. Herein, we summarize and discuss recent developments in RR applications aimed to link the structure-function relationship of heme proteins within biological systems, connected, e.g., with the formation of hemoglobin (Hb) adducts (nitrosylhemoglobin, cyanhemoglobin, sulfhemoglobin), irreversible Hb alterations deteriorating oxygen binding and differentiation of heme proteins oxidation state within live cells in situ.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 3","pages":"Article 141065"},"PeriodicalIF":2.5,"publicationDate":"2025-02-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143497595","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}

{"title":"DSP-1, the major fibronectin type-II protein of donkey seminal plasma is a small heat-shock protein and exhibits chaperone-like activity against thermal and oxidative stress","authors":"Sk Alim ,&nbsp;Sudheer K. Cheppali ,&nbsp;Sonali S. Pawar,&nbsp;Musti J. Swamy","doi":"10.1016/j.bbapap.2025.141064","DOIUrl":"10.1016/j.bbapap.2025.141064","url":null,"abstract":"<div><div>Fibronectin type-II (FnII) proteins are major constituents in the seminal plasma of many mammals and play a crucial role in sperm capacitation. Additionally, the seminal FnII proteins from bull and horse exhibit chaperone-like activity (CLA), by acting as small heat shock proteins (<em>shsp</em>s). The present work demonstrates that the major FnII protein of donkey seminal plasma, DSP-1 exhibits CLA with broad specificity and protects various client proteins such as alcohol dehydrogenase, lactate dehydrogenase and enolase against thermal and oxidative stress. Binding of phosphorylcholine (PrC) – the head group moiety of choline phospholipids, which are the physiological ligands of DSP-1 – decreased the CLA whereas binding of 1,2-dioleoyl-<em>sn</em>-glycero-3-phospholcholine (DOPC) increased the CLA. Biophysical studies suggested that these contrasting effects on the CLA by phosphorylcholine and diacyl phosphatidylcholine could be attributed to changes in the surface hydrophobicity of DSP-1 upon binding to these ligands. Interestingly, binding of PrC reduced DSP-1 tetramers to monomers with lower surface hydrophobicity, whereas binding to DOPC liposomes increased its surface hydrophobicity. These results, which demonstrate that DSP-1 exhibits CLA and functions as a molecular chaperone, expand the family of mammalian seminal FnII proteins that function as <em>shsp</em>s.</div></div>","PeriodicalId":8760,"journal":{"name":"Biochimica et biophysica acta. Proteins and proteomics","volume":"1873 3","pages":"Article 141064"},"PeriodicalIF":2.5,"publicationDate":"2025-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143432278","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}