58607-69-5Relevant academic research and scientific papers
Search for fibrous aggregates potentially useful in regenerative medicine formed under physiological conditions by self-assembling short peptides containing two identical aromatic amino acid residues
Fraczyk, Justyna,Lipinski, Wojciech,Chaberska, Agata,Wasko, Joanna,Rozniakowski, Kamil,Kaminski, Zbigniew J.,Bogun, Maciej,Draczynski, Zbigniew,Menaszek, Elzbieta,Stodolak-Zych, Ewa,Kaminska, Marta,Kolesinska, Beata
supporting information, (2018/03/21)
This study investigates the propensity of short peptides to self-organize and the influence of aggregates on cell cultures. The dipeptides were derived from both enantiomers of identical aromatic amino acids and tripeptides were prepared from two identica
D -amino acids boost the selectivity and confer supramolecular hydrogels of a nonsteroidal anti-inflammatory drug (NSAID)
Li, Jiayang,Kuang, Yi,Gao, Yuan,Du, Xuewen,Shi, Junfeng,Xu, Bing
supporting information, p. 542 - 545 (2013/03/14)
As systemically used therapeutics for treating acute or chronic pains or inflammations, nonsteroidal anti-inflammatory drugs (NSAIDs) also associate with the adverse gastrointestinal and renal effects and cardiovascular risks. Thus, it is beneficial to develop topical gels that selectively inhibit cyclooxygenase-2 (COX-2) for the management of local inflammation. In this work, we demonstrate that the covalent conjugation of d-amino acids to naproxen (i.e., a NSAID) not only affords supramolecular hydrogelators for the topical gels but also unexpectedly and significantly elevates the selectivity toward COX-2 about 20× at little expense of the activity of naproxen. This work illustrates a previously unexplored approach that employs d-amino acids for the development of functional molecules that have dual or multiple roles and exceptional biostability, which offers a new class of molecular hydrogels of therapeutic agents.
Aminolytic reaction catalyzed by d-stereospecific amidohydrolases from Streptomyces spp
Arima, Jiro,Ito, Hitomi,Hatanaka, Tadashi,Mori, Nobuhiro
experimental part, p. 1460 - 1469 (2012/01/12)
From investigation of 2000 soil isolates, we identified two serine-type amidohydrolases that can hydrolyze d-aminoacyl derivatives from the culture supernatant of Streptomyces species 82F2 and 83D12. The enzymes, redesignated as 82F2-DAP and 83D12-DAP, were purified for homogeneity and characterized. Each enzyme had molecular mass of approximately 40 kDa, and each showed moderate stability with respect to temperature and pH. Among hydrolytic activities toward d-aminoacyl-pNAs, the enzymes showed strict specificity toward d-Phe-pNA, but showed broad specificity toward d-aminoacyl esters. The specific activity for d-Phe-pNA hydrolysis of 82F2-DAP was ten-fold higher than that of 83D12-DAP. As a second function, each enzyme showed peptide bond formation activity by its function of aminolysis reaction. Based on results of d-Phe-d-Phe synthesis under various conditions, we propose a reaction mechanism for d-Phe-d-Phe production. Furthermore, the enzymes exhibited peptide elongation activity, producing oligo homopeptide in a one-pot reaction. We cloned the genes encoding each enzyme, which revealed that the primary structure of each enzyme showed 30-60% identity with those of peptidases belonging to the clan SE, S12 peptidase family categorized as serine peptidase with d-stereospecificity.
Peptide bond formation by aminolysin-A catalysis: A simple approach to enzymatic synthesis of diverse short oligopeptides and biologically active puromycins
Usuki, Hirokazu,Yamamoto, Yukihiro,Arima, Jiro,Iwabuchi, Masaki,Miyoshi, Shozo,Nitoda, Teruhiko,Hatanaka, Tadashi
supporting information; experimental part, p. 2327 - 2335 (2011/05/02)
A new S9 family aminopeptidase derived from the actinobacterial thermophile Acidothermus cellulolyticus was cloned and engineered into a transaminopeptidase by site-directed mutagenesis of catalytic Ser491 into Cys. The engineered biocatalyst, designated aminolysin-A, can catalyze the formation of peptide bonds to give linear homo-oligopeptides, hetero-dipeptides, and cyclic dipeptides using cost-effective substrates in a one-pot reaction. Aminolysin-A can recognize several C-terminal-modified amino acids, including the l- and d-forms, as acyl donors as well as free amines, including amino acids and puromycin aminonucleoside, as acyl acceptors. The absence of amino acid esters prevents the formation of peptides; therefore, the reaction mechanism involves aminolysis and not a reverse reaction of hydrolysis. The aminolysin system will be a beneficial tool for the preparation of structurally diverse peptide mimetics by a simple approach.
