Peptide research最新文献_第6页

Modification of the carboxyl terminal group affects replacement set analysis of a cytotoxic T cell epitope. 羧基末端基团的修饰影响细胞毒性T细胞表位的置换集分析。

Peptide research Pub Date : 1995-09-01

A Suhrbier, S R Burrows, J Gardner, S Rodda

引用次数: 0

Cleavage and deprotection of peptide resins using chloro- and bromotrialkylsilanes. 氯基和溴基三烷基硅烷对肽树脂的裂解和脱保护。

Peptide research Pub Date : 1995-09-01

J L Hughes, E J Leopold

引用次数: 0

A synthetic peptide corresponding to glycoprotein hormone alpha subunit residues 32-46 inhibits gonadotropin binding to receptor. 与糖蛋白激素α亚基残基32-46相对应的合成肽抑制促性腺激素与受体的结合。

Peptide research Pub Date : 1995-09-01

N Leng, P Grasso, M R Deziel, L E Reichert

{"title":"A synthetic peptide corresponding to glycoprotein hormone alpha subunit residues 32-46 inhibits gonadotropin binding to receptor.","authors":"N Leng, P Grasso, M R Deziel, L E Reichert","doi":"","DOIUrl":"","url":null,"abstract":"A synthetic peptide strategy was used to study structure-function relationships between residues 32 to 46 of the glycoprotein hormone alpha subunit (GPH alpha) and the testicular follicle-stimulating hormone (FSH) and luteinizing hormone (LH/hCG) receptors. A peptide amide corresponding to this region [GPH-alpha-(32-46)] inhibited both 125I-hFSH and 125I-hCG binding to their respective calf testis membrane receptors. The concentration at which GPH-alpha-(32-46) peptide amide inhibited FSH binding by 50% (IC50) was 36 microM, and for hCG it was 54 microM. GPH-alpha-(32-46) peptide amide also inhibited FSH-stimulated estradiol biosynthesis in cultured rat Sertoli cells. In order to determine the involvement of individual residues within this region of the glycoprotein hormone alpha subunit in receptor binding inhibitory activity, truncated and alanine-substituted peptide analogs were synthesized and tested in both FSH and hCG radioligand receptor competition assays. Based on the relative potency of each peptide, we conclude that Phe-33, Arg-35, Arg-42, Ser-43 and Lys-44 may be important, and Cys-32 is required, for inhibition of FSH and hCG binding to their respective receptor. Our results demonstrate involvement of the glycoprotein hormone alpha-subunit in receptor binding, identify residues 32 to 46 as a receptor binding domain, and define the relative importance of specific residues within this region of the alpha subunit for hormone-receptor interaction.","PeriodicalId":20005,"journal":{"name":"Peptide research","volume":"8 5","pages":"272-7"},"PeriodicalIF":0.0,"publicationDate":"1995-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19569194","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

(S)-C alpha-ethyl, C alpha-benzylglycine [(S)-(alpha Et)Phe] peptides fold in left-handed helical structures. (S)-C α -乙基，C α -苄基甘氨酸[(S)-(α Et)Phe]多肽以左旋螺旋结构折叠。

Peptide research Pub Date : 1995-09-01

M Doi, T Ishida, A Polese, F Formaggio, M Crisma, C Toniolo, Q B Broxterman, J Kamphuis

引用次数: 0

Selective effects of charge on G protein activation by FSH-receptor residues 551-555 and 650-653. 电荷对fsh受体残基551-555和650-653活化G蛋白的选择性影响

Peptide research Pub Date : 1995-09-01

P Grasso, M R Deziel, L E Reichert

{"title":"Selective effects of charge on G protein activation by FSH-receptor residues 551-555 and 650-653.","authors":"P Grasso, M R Deziel, L E Reichert","doi":"","DOIUrl":"","url":null,"abstract":"Two cytosolic regions of the rat testicular FSH receptor (FSHR), residues 533-555 and 645-653, have been identified as G protein-coupling domains. We localized the activity in these domains to their C-terminal sequences, residues 551-555 (KIAKR, net charge +3) and 650-653 (RKSH, net charge +3), and examined the effects of charge on G protein activation by the C-terminal peptides, using synthetic analogs containing additions, through alanine (A) linkages, of arginine (R, +), histidine (H, +) or both. RA-KIAKR (net charge +4) mimicked the effect of FSHR-(551-555) on guanine nucleotide exchange in rat testis membranes, but reduced its ability to inhibit FSH-stimulated estradiol biosynthesis in cultured rat Sertoli cells. Further increasing net charge by the addition of H (HARA-KIAKR, net charge +5) increased guanosine 5'-triphosphate (GTP) binding, but eliminated FSHR-(551-555) effects on FSH-stimulated steroidogenesis. HA-RKSH (net charge +4) significantly inhibited guanine nucleotide exchange in rat testis membranes, but stimulated basal and potentiated FSH-induced estradiol biosynthesis in cultured rat Sertoli cells. Addition of two H residues (HAHA-RKSH, net charge +5) restored GTP binding and further potentiated basal and FSH-stimulated steroidogenesis. These results suggest that positive charges in G protein-coupling domains of the FSHR play a role in modulating G protein activation and postbinding effects of FSH, such as steroidogenesis.","PeriodicalId":20005,"journal":{"name":"Peptide research","volume":"8 5","pages":"278-84"},"PeriodicalIF":0.0,"publicationDate":"1995-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19569286","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Glycosaminoglycan specificity of a heparin-binding peptide. 肝素结合肽的糖胺聚糖特异性。

Peptide research Pub Date : 1995-09-01

G J Taylor, S C Yorke, D R Harding

{"title":"Glycosaminoglycan specificity of a heparin-binding peptide.","authors":"G J Taylor, S C Yorke, D R Harding","doi":"","DOIUrl":"","url":null,"abstract":"Glycosaminoglycans are complex sulfated polysaccharides with a diverse range of biological functions. Three glycosaminoglycan standards--chondroitin sulfate, dermatan sulfate and heparin--were characterized during this study. The interaction of the heparin binding site of protein C inhibitor, represented by the peptide sequence 264-283, in solution with the above glycosaminoglycan standards was studied. Circular dichroism spectroscopy was used to determine the dominant secondary structure induced in the peptide upon binding the relevant glycosaminoglycans. The various glycosaminoglycans induced different secondary structures. The level of induced secondary structure by dermatan sulfate and heparin was approximately twice that induced by chondroitin sulfate. For chondroitin sulfate and heparin, alpha-helix was the dominant ordered secondary structure, whereas for dermatan sulfate the beta-strand conformation dominated. The order of secondary structure induction of the protein C inhibitor peptide by the glycosaminoglycans paralleled the reported biological activities of these glycosaminoglycans for mediation of the biological activity in the intact protein. The strength of the interaction of dermatan sulfate and heparin with the protein C inhibitor peptide was measured by determining the concentration of salt required to inhibit 50% of the interaction. The values determined were 0.1 and 0.3 M salt for dermatan sulfate and heparin, respectively. These results show that different glycosaminoglycans can support different secondary structures in the protein C inhibitor peptide.","PeriodicalId":20005,"journal":{"name":"Peptide research","volume":"8 5","pages":"286-93"},"PeriodicalIF":0.0,"publicationDate":"1995-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19569195","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Synthesis of an O-palmitoylated 44-residue peptide amide (PLTX II) blocking presynaptic calcium channels in Drosophila. 阻断果蝇突触前钙通道的o -棕榈酰化44-残基肽酰胺(PLTX II)的合成。

Peptide research Pub Date : 1995-07-01

J Bódi, H Nishio, Y Zhou, W D Branton, T Kimura, S Sakakibara

{"title":"Synthesis of an O-palmitoylated 44-residue peptide amide (PLTX II) blocking presynaptic calcium channels in Drosophila.","authors":"J Bódi, H Nishio, Y Zhou, W D Branton, T Kimura, S Sakakibara","doi":"","DOIUrl":"","url":null,"abstract":"PLTX II, a presynaptic calcium channel blocker in Drosophila isolated from the plectreurys spider venom, is a 44-residue peptide containing ten Cys residues and an O-palmitoylated threonine amide at the carboxy-terminus. In this study, the palmitoylated peptide was synthesized in solution by applying our maximum protection strategy using the HF method at the final deprotecting step. Before designing the synthesis, we examined the stability of the palmitoyl moiety under the conditions for the synthesis of the peptide using several model peptides. The O-palmitoyl group was confirmed to be stable during elongation of the peptide bonds, but was partially removable during the deprotection reaction in HF. The depalmitoylation reaction in HF was temperature- and time-dependent. Therefore, the decision was made to protect the Asp residues with benzyl ester, since it is more susceptible to HF than cyclohexyl ester, which is now commonly used in the Boc-based, solid-phase synthesis. Thus, the HF reaction was carried out at -10 degrees or -15 degrees C for 1 h in order to reduce the extent of the depalmitoylation reaction. The resulting palmitoylated and depalmitoylated products were separated, the remaining Acm groups were removed using Hg(OAc)2, and then the completely deprotected peptides were folded to their native forms. The final palmitoylated peptide was proven to be identical with the natural one using various HPLC systems and by bioassay.(ABSTRACT TRUNCATED AT 250 WORDS)","PeriodicalId":20005,"journal":{"name":"Peptide research","volume":"8 4","pages":"228-35"},"PeriodicalIF":0.0,"publicationDate":"1995-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19509644","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Detection of secondary amines on solid phase. 固相法仲胺的检测。

Peptide research Pub Date : 1995-07-01

T Vojkovsky

引用次数: 0

Linear presentation of variable side-chain spacing in a highly diverse combinatorial library. 高度多样化组合库中可变侧链间距的线性表示。

Peptide research Pub Date : 1995-07-01

V Krchnák, A S Weichsel, D Cabel, M Lebl

引用次数: 0

Structure of human calcitonin gene-related peptide (hCGRP) and of its antagonist hCGRP 8-37 as determined by NMR and molecular modeling. 人降钙素基因相关肽(hCGRP)及其拮抗剂hCGRP 8-37的结构研究

Peptide research Pub Date : 1995-07-01

Y Boulanger, A Khiat, Y Chen, L Senécal, Y Tu, S St-Pierre, A Fournier

{"title":"Structure of human calcitonin gene-related peptide (hCGRP) and of its antagonist hCGRP 8-37 as determined by NMR and molecular modeling.","authors":"Y Boulanger, A Khiat, Y Chen, L Senécal, Y Tu, S St-Pierre, A Fournier","doi":"","DOIUrl":"","url":null,"abstract":"The solution structures of human calcitonin gene-related peptide (hCGRP, 37 residues) and of its antagonistic fragment hCGRP 8-37 have been determined by two-dimensional 1H nuclear magnetic resonance (NMR) spectroscopy and molecular modeling. Analysis of the double quantum filtered correlation spectroscopy, total correlation spectroscopy and nuclear Overhauser enhancement spectroscopy spectra led to a complete assignment and to the identification of more than 350 intra- and interresidue connectivities for each peptide. Molecular models were calculated by molecular dynamics and energy minimization using distance constraints. The structure of hCGRP is characterized by a rigid N-terminal disulfide-bonded loop followed by helix segments (Val8-Leu16), a gamma-turn (Ser19-Gly21) and several local hydrogen-bonded patterns. The structure of hCGRP 8-37 is less defined than the structure of hCGRP and no helix structure is present. Molecular models of both peptides are consistent with the NH temperature coefficients and secondary chemical shifts of the alpha-protons. Hydrogen bonding with the disulfide-bonded ring appears to be critical for helix formation, both structural elements being essential for agonistic activity.","PeriodicalId":20005,"journal":{"name":"Peptide research","volume":"8 4","pages":"206-13"},"PeriodicalIF":0.0,"publicationDate":"1995-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19509641","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0