Nmr study of poly(aspartic acid). I. α- and β-Peptide bonds in poly(aspartic acid) prepared by thermal polycondensation

Biopolymers ◽  
1981 ◽  
Vol 20 (8) ◽  
pp. 1605-1614 ◽  
Author(s):  
H. Pivcová ◽  
V. Saudek ◽  
J. Drobník ◽  
J. Vlasák
Keyword(s):  
Aspartic Acid ◽  
Peptide Bonds ◽  
Nmr Study ◽  
Thermal Polycondensation

Nmr study of poly(aspartic acid). II. α- and β-Peptide bonds in poly(aspartic acid) prepared by common methods

Biopolymers ◽  
1981 ◽  
Vol 20 (8) ◽  
pp. 1615-1623 ◽  
Author(s):  
V. Saudek ◽  
H. Pivcová ◽  
J. Drobník
Keyword(s):  
Aspartic Acid ◽  
Peptide Bonds ◽  
Nmr Study

scholarly journals Thermal Synthesis of Polypeptides from N-Butyloxycarbonyl Oligopeptides Containing Aspartyl Residue at C-Terminus

2017 ◽  
Vol 2017 ◽  
pp. 1-16
Author(s):  
Toratane Munegumi ◽  
Takafumi Yamada
Keyword(s):  
Aspartic Acid ◽  
Organic Synthesis ◽  
Prebiotic Chemistry ◽  
Average Molecular Weight ◽  
Carboxyl Terminus ◽  
Peptide Bonds ◽  
Thermal Synthesis ◽  
Thermal Reactions ◽  
C Terminus ◽  
Aspartyl Residue

The thermal reactions of amino acids have been investigated for pure organic synthesis, materials preparation in industry, and prebiotic chemistry. N-t-Butyloxycarbonyl aspartic acid (Boc-Asp) releases 2-butene and carbon dioxide upon heating without solvents. The resulting mixture of the free molten aspartic acid was dehydrated to give peptide bonds. This study describes the thermal reactions of N-t-butyloxycarbonyl peptides (Boc-Gly-L-Asp, Boc-L-Ala-L-Asp, Boc-L-Val-L-Asp, and Boc-Gly-Gly-L-Asp) having an aspartic residue at the carboxyl terminus. The peptides were deprotected upon heating at a constant temperature between 110 and 170°C for 1 to 24 h to afford polypeptides in which the average molecular weight reached 7800.

Kinetics of solid phase thermal polycondensation of aspartic acid in evacuated system

2013 ◽  
Vol 83 (11) ◽  
pp. 2046-2049 ◽  
Author(s):  
V. A. Yablokov ◽  
Ya. A. Vasina ◽  
I. D. Grishin
Keyword(s):  
Aspartic Acid ◽  
Solid Phase ◽  
Thermal Polycondensation ◽  
Kinetics Of

scholarly journals Crystal structure of N-{N-[N-(tert-butoxycarbonyl)-L-α-aspartyl]-L-α-aspartyl}-L-α-aspartic acid 14,24,34-trimethyl ester 31-2-oxo-2-phenylethyl ester {Boc-[Asp(OMe)]3-OPac}

2019 ◽  
Vol 75 (5) ◽  
pp. 585-588
Author(s):  
Takuma Kato ◽  
Saki Kishimoto ◽  
Akiko Asano ◽  
Mitsunobu Doi
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bonds ◽  
Aspartic Acid ◽  
Protecting Group ◽  
Peptide Bonds ◽  
Axis Direction ◽  
Sheet Structure ◽  
Β Sheet

In the title homotripeptide {Boc-[Asp(OMe)]3-OPac}, C28H37N3O13, all peptide bonds adopt an s-trans conformation with respect to the N—H and C=O groups. In the crystal, N—H...O hydrogen bonds result in an infinite parallel β-sheet structure running along the b-axis direction. The Boc protecting group at the N-terminus of the peptide is disordered over two sites with occupancy factors of 0.504 (5) and 0.496 (5).

Synthesis of the carboxy-terminal octapeptide of cholecystokinin (CKK-8) based on incorporation of O4-sulfotyrosine by enzymatically catalyzed formation of peptide bonds

1988 ◽  
Vol 53 (5) ◽  
pp. 1086-1093 ◽  
Author(s):  
Václav Čeřovský ◽  
Jan Hlaváček ◽  
Jiřina Slaninová ◽  
Karel Jošt
Keyword(s):  
Aspartic Acid ◽  
Sodium Salt ◽  
Proteolytic Enzymes ◽  
Biological Activities ◽  
Proteinase K ◽  
Side Chain ◽  
Peptide Fragments ◽  
Peptide Bonds ◽  
Carboxy Terminal ◽  
Amide Fragment

Papain-catalyzed condensation of sodium salt of tert-butyloxycarbonyl-β-tert-butyloxyaspartyl-O4-sulfotyrosine (fragment 1-2) with methionyl-glycyl-tryptophyl-methionyl-aspartyl-phenylalanine amide (fragment 3-8) has been elaborated. Deprotection of the thus-obtained octapeptide afforded CCK-8 which exhibited full biological activities. Benzyloxycarbonylaspartyl-phenylalanine amide (fragment 7-8) was prepared using thermolysin without protecting the aspartic acid side chain. Attempted condensation of tert-butyloxycarbonylmethionyl-glycyl-tryptophan (fragment 3-5) with methionyl-aspartyl-phenylalanine amide (fragment 6-8), catalyzed by α-chymotrypsin, subtilisin or proteinase K, afforded the product (fragment 3-8) in only low yields. Further use of proteolytic enzymes for preparing other peptide fragments of the CCK-8 molecule without side chain protection is investigated.

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