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

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

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.

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.

1H-NMR Study of the Intramolecular Interaction of a Substrate Analogue Covalently Attached to Aspartic Acid-101 in Lysozyme1

1991 ◽  
Vol 109 (5) ◽  
pp. 690-698 ◽  
Author(s):  
Tadashi Ueda ◽  
Yoshimasa Isakari ◽  
Hidenori Aoki ◽  
Takanori Yasukochi ◽  
Shun-ichi Masutomo ◽  
...  
Keyword(s):  
Aspartic Acid ◽  
1H Nmr ◽  
Intramolecular Interaction ◽  
Substrate Analogue ◽  
Nmr Study

scholarly journals Thermal decomposition of the amino acids glycine, cysteine, aspartic acid, asparagine, glutamic acid, glutamine, arginine and histidine

2017 ◽  
Author(s):  
Ingrid M. Weiss ◽  
Christina Muth ◽  
Robert Drumm ◽  
Helmut O.K. Kirchner
Keyword(s):  
Mass Spectrometry ◽  
Amino Acids ◽  
Thermal Decomposition ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Peptide Bonds ◽  
Integer Coefficients ◽  
Half Integer ◽  
Volatile Products

AbstractCalorimetry, thermogravimetry and mass spectrometry were used to follow the thermal decomposition of the eight amino acids G, C, D, N, E, Q, R and H between 185°C and 280°C. Endothermic heats of decomposition between 72 and 151 kJ/mol are needed to form 12 to 70 % volatile products. This process is neither melting nor sublimation. With exception of cysteine they emit mainly H2O, some NH3 and no CO2. Cysteine produces CO2 and little else. The reactions are described by polynomials, AA ^ a (NH3) + b (H2O) + c (CO2) + d (H2S) + e (residue), with integer or half integer coefficients. The solid monomolecular residues are rich in peptide bonds.

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