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Peptides Containing (peptide + containing)

Distribution by Scientific Domains
Chemistry66%
Life Sciences33%

Selected Abstracts

Synthesis of IB-01211, a Cyclic Peptide Containing 2,4-Concatenated Thia- and Oxazoles, via Hantzsch Macrocyclization.

CHEMINFORM, Issue 30 2007
Delia Hernandez
Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF. [source]

Cyrmenins, Novel Antifungal Peptides Containing a Nitrogen-Linked ,-Methoxyacrylate Pharmacophore: Isolation and Structural Elucidation

EUROPEAN JOURNAL OF ORGANIC CHEMISTRY, Issue 2 2004
Thomas Leibold
Abstract The novel antifungal metabolites cyrmenin A, B1, and B2 (1,3) were isolated from Archangium gephyra and Cystobacter armeniaca strains (myxobacteria). The cyrmenins are modified N -acyldipeptide esters containing a didehydroalanine, a 3- O -methyl-didehydroserine and a (2E,4Z)-undecadienoic or -dodecadienoic acid residue. These compounds represent the first bacterial counterparts of strobilurins that are characterized by an ,-substituted ,-methoxyacrylate pharmacophore. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2004) [source]

Facile Synthesis and Cleavage of Imidazolidines in a Novel Protection Strategy for the Preparation of Peptides Containing a Reduced Amide Bioisostere.

CHEMINFORM, Issue 15 2003
Jun Zhao
Abstract For Abstract see ChemInform Abstract in Full Text. [source]

The Proteolytic Stability of ,Designed' , -Peptides Containing , -Peptide-Bond Mimics and of Mixed ,,, -Peptides: Application to the Construction of MHC-Binding Peptides

CHEMISTRY & BIODIVERSITY, Issue 5 2005
David
Whereas , -peptides are rapidly degraded in vivo and in vitro by a multitude of peptidases, substrates constructed entirely of or incorporating homologated , -amino acid (i.e., , -amino acid) units exhibit a superior stability profile. Efforts made so far to proteolytically hydrolyze a ,, peptide bond have not proved fruitful; a study aimed at breaching this proteolytic stability is discussed here. A series of such bonds have been designed with side-chain groups similar in relative positions (constitution) and three-dimensional arrangements (configuration) as found about , -peptidic amide bonds. Increasing the prospect for degradation would permit the tuning of , -peptide stability; here, however, no cleavage was observed (1, 2, 4,6, Table,1). Peptides comprised of , - and , -amino acids (mixed ,,, -peptides, 8,11) are expected to benefit from both recognition by a natural receptor and a high level of proteolytic stability, ideal characteristics of pharmacologically active compounds. ,3 -Peptides containing , -amino acid moieties at the N-terminus are degraded, albeit slowly, by several peptidases. Of particular interest is the ability of pronase to cleave an ,, peptide bond, namely that of ,Ala,3hAla. Significantly, successful hydrolysis is independent of the configuration of the , -amino acid. Some of the ,,, -peptides discussed here are being investigated for their binding affinities to class I MHC proteins. The computer-programming steps required to prepare ,,, -peptides on an automated peptide synthesizer are presented. [source]

Stage-dependent and alternative splicing of sGnRH messengers in rainbow trout testis during spermatogenesis

MOLECULAR REPRODUCTION & DEVELOPMENT, Issue 1 2001
Svetlana Uzbekova
Abstract The gonadotropin releasing hormone (GnRH) has long been considered as a neuropeptide involved in the control of the reproductive cycle. However, the presence of GnRH and its receptors in various tissues, including ovary and testis, suggests a role as autocrine/paracrine factor. In the present study, we report the expression of the sGnRH-1 and sGnRH-2 genes encoding salmon GnRH in rainbow trout testis throughout testicular development and spermatogenesis. We demonstrate that both sGnRH mRNA are expressed prior of sexual differentiation. In adult, northern blot analysis indicates that sGnRH-2 transcripts are expressed in the testis at higher levels than sGnRH-1 messengers. Moreover, we observed that the expression of sGnRH-2, and not sGnRH-1, messengers was stage-dependent. sGnRH-2 mRNA expression decreases at the onset and progressively rebounds at the end of spermatogenesis. In addition, we demonstrate that a complex stage-dependent and differential splicing of the sGnRH-2 messengers occurs throughout spermatogenesis. We isolated five transcripts corresponding to sGnRH-2 messengers. Two of them may encode a novel and shortened GnRH-associated peptide containing 18 residues instead of 46. Our data provide new insight in the putative role of GnRH and GAP peptides as autocrine/paracrine factors of spermatogenesis. Mol. Reprod. Dev. 59:1,10, 2001. © 2001 Wiley-Liss, Inc. [source]

Regulation of the catalytic behaviour of L-form starch phosphorylase from sweet potato roots by proteolysis

PHYSIOLOGIA PLANTARUM, Issue 4 2002
Han-Min Chen
Starch phosphorylase (SP) is an enzyme used for the reversible phosphorolysis of the ,-glucan in plant cells. When compared to its isoform in an animal cell, glycogen phosphorylase, a peptide containing 78 amino acids (L78) is inserted in the centre of the low-affinity type starch phosphorylase (L-SP). We found that the amino acid sequence of L78 had several interesting features including the presence of a PEST region, which serves as a signal for rapid degradation. Indeed, most L-SP molecules isolated from mature sweet potato roots were nicked in the middle of a molecule, but still retained their tertiary or quaternary structures, as well as full catalytic activity. The nicking sites on the L78 were identified by amino acid sequencing of these peptides, which also enabled us to propose a proteolytic process for L-SP. Enzyme kinetic studies of L-SP in the direction of starch synthesis indicated that the Km decreased during the proteolytic process when starch was used as the limiting substrate, but the Km for the other substrate (Glc-1-P) increased. On the other hand, the maximum velocities (Vmax) increased for both substrates. Mobility of the nicked L-SP was retarded on a native polyacrylamide gel containing soluble starch, indicating the increased affinity for starch. Results in this study suggested that L78 and its proteolytic modifications might play a regulatory role on the catalytic behaviour of L-SP in starch biosynthesis. [source]