3918-87-4Relevant articles and documents
A dynamic combinatorial library for biomimetic recognition of dipeptides in water
Klepel, Florian,Ravoo, Bart Jan
supporting information, p. 1588 - 1595 (2020/09/16)
Small peptides are involved in countless biological processes. Hence selective binding motifs for peptides can be powerful tools for labeling or inhibition. Finding those binding motifs, especially in water which competes for intermolecular H-bonds, poses an enormous challenge. A dynamic combinatorial library can be a powerful method to overcome this issue. We previously reported artificial receptors emerging form a dynamic combinatorial library of peptide building blocks. In this study we aimed to broaden this scope towards recognition of small peptides. Employing CXC peptide building blocks, we found that cyclic dimers of oxidized CFC bind to the aromatic peptides FF and YY (K ≈ 229-702 M-1), while AA binds significantly weaker (K ≈ 65-71 M-1).
γ-Valerolactone (GVL): An eco-friendly anchoring solvent for solid-phase peptide synthesis
Al Musaimi, Othman,El-Faham, Ayman,Basso, Alessandra,de la Torre, Beatriz G.,Albericio, Fernando
, (2019/08/26)
Due to the hazardous nature of CH2Cl2, regulatory authorities have imposed restrictions to minimize or even stop its use. It has therefore become imperative to identify environmentally benign solvents to replace it. Here we report on a bio derived solvent, γ-valerolactone, for the incorporation of the first amino acid onto p-alkoxybenzyl alcohol resin in solid-phase peptide synthesis. Satisfactory loading values (by a spectrophotometric method) were achieved. Furthermore, racemization and dipeptide formation were also checked and found to be acceptable.
Branched peptide linkers
-
, (2008/06/13)
Conjugates containing a targeting ligand, such as an antibody, a therapeutically active drug and a branched peptide linker. The branched peptide linker contains two or more amino acid moieties that provide an enzyme cleavage site. The number of drugs capable of being bonded to the branched linkers varies by a factor of two for each generation of branching.
Enantioselective Enzymatic Cleavage of N-Benzyloxycarbonyl Groups
Patel, Ramesh N.,Nanduri, Venkata,Brzozowski, David,McNamee, Clyde,Banerjee, Amit
, p. 830 - 834 (2007/10/03)
A new enzymatic process for the enantioselective cleavage of N-benzyloxycarbonyl (Cbz) groups from protected amino acids and related compounds has been developed. The Cbz-deprotecting enzyme was isolated from cell extracts of Sphingomonas paucimobilis SC 16113 and purified to homogeneity. The purified protein has a molecular weight of 155,000 daltons and a subunit size of 44,000 daltons.
Selective deprotection of phthalyl protected amines
Costello, Colleen A.,Kreuzman, Adam J.,Zmijewski, Milton J.
, p. 7469 - 7472 (2007/10/03)
Phthalyl amidase selectively deprotects phthalimido groups under very mild aqueous conditions in a one-pot reaction to produce phthalic acid and the free amine. The enzyme has been shown to deprotect several primary amines of distinctly different structure, and exhibits chiral selectivity when the substrate contains extensive β-branching. The enzyme has a definite requirement for ortho positioning of the functional groups on a fixed axis of rotation.
NEW APPROACHES TO THE ASYMMETRIC SYNTHESIS OF NON-PROTEINOGENIC α-AMINO ACIDS AND DIPEPTIDES THROUGH CHIRAL β-LACTAM INTERMEDIATES
Ojima, Iwao,Chen, Hauh-Jyun C.,Qiu, Xiaogang
, p. 5307 - 5318 (2007/10/02)
Novel and effective routes to optically pute aromatic α-amino acids, α-methyl-α-amino acids and their derivatives including dipeptides are developed via homochiral β-lactams which are obtained through asymmetric cycloadditions of ketenes to imines.
Mechanism of Dipeptidyl Carboxypeptidase Activity of Thermolysin
Fukuda, Mitsuhiro,Kunugi, Shigeru
, p. 2965 - 2970 (2007/10/02)
Steady state and presteady state kinetic analyses were performed for thermolysin-catalysed hydrolysis of chromophoric tripeptide substrates with free carboxyl terminal.The pH dependence of kcat showed fairly higher pKa (ca.7) than that of the second-order rate parameter (kcat/Km)(ca.5) and the pH-dependence of Km resembled that of Ki for N-blocked dipeptidyl inhibitor observed before (S.Kunigi et al.Eur.J.Biochem. 124, 157 (1982)).These findings indicated that the reaction with this type of substrate involves a nonproductive binding mode.In a presteady state kinetic study by stopped-flow method, a burst process of 10-20 ms order was observed before the linear steady state at a relatively low pH and temperature.This process showed moderate pH dependence.Considering these experimental results coupled with those accumulated so far on this enzyme, a unified mechanism including a nonproductive binding and an isomerization process in prior to the cleavage of the peptide bond was proposed for the dipeptidyl carboxypeptidase activity of this enzyme.
The Steric Hindrance of the Stepwise Reaction of N-Carboxy α-Amino Acid Anhydride with the α-Amino Acid Ester
Oya, Masanao,Takahashi, Tomoko
, p. 2705 - 2707 (2007/10/02)
The mechanisms of the reactions of 4-alkyloxazolidinediones (1) (N-carboxy α-amino acid anhydrides(NCAs)) with α-amino acid benzyl ester p-toluenesulfonates (2) were investigated in acetonitrile containing triethylamine at low and room temperatures.Two types of reactions were observed: (1) the polymerization of NCAs was initiated with a small amount of 2 to produce polypeptides (6), and (2) the dipeptide benzyl esters (4) were produced by the stepwise reaction of NCAs with the esters.Both the polymerization and the dipeptide formation (1+2) seemed to be initiated by the nucleophilic attack of the amino group of the ester on the C-5 carbon of NCAs.The polymerization proceeded when the side chains of the amino acid esters (R2) were more bulky than those of the NCAs (R1).On the contrary, dipeptide esters were produced when the side chains of the NCAs (R1) were more bulky than those of the esters (R2).
