scholarly journals Synthesis and properties of peptidyl derivatives of arginylfluoromethanes

1988 ◽  
Vol 256 (2) ◽  
pp. 481-486 ◽  
Author(s):  
H Angliker ◽  
P Wikström ◽  
P Rauber ◽  
S Stone ◽  
E Shaw
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site ◽  
Relative Effectiveness ◽  
Serine Proteinases ◽  
Cysteine Proteinases ◽  
Peptide Derivatives ◽  
Guanidino Group ◽  
Derivatives Of

Two peptide derivatives of arginylfluoromethane (Arg-CH2F), namely Bz(benzoyl)-Phe-ArgCH2F and D-Phe-Pro-Arg-CH2F, have been synthesized by extension of available methods, i.e. the Dakin-West reaction [Rasnick (1985) Anal. Biochem. 149, 461-465] or synthesis of a phthaloyl-blocked C-terminal fluoromethane [Rauber, Angliker, Walker & Shaw (1986) Biochem. J. 239, 633-640; Angliker, Wikström, Rauber & Shaw (1987) Biochem. J. 241, 871-875] with subsequent elongation. The guanidino group of arginine was protected as the bis-Cbz (benzyloxycarbonyl) derivative. The products were examined as active-site-directed inhibitors of some trypsin-related serine proteinases as well as a pair of cysteine proteinases. The results extend previous observations that the rate of alkylation of serine proteinases by fluoromethanes may be considerably slower than by chloromethanes. As expected, the amino acid sequence of the inhibitors influenced their relative effectiveness. Thus the rate of inactivation of a number of trypsin-like proteinases by D-Phe-Pro-Arg-CH2F varied by more than two orders of magnitude.

scholarly journals Derived amino acid sequence and identification of active site residues of Escherichia coli beta-hydroxydecanoyl thioester dehydrase.

1988 ◽  
Vol 263 (10) ◽  
pp. 4641-4646 ◽  
Author(s):  
J E Cronan ◽  
W B Li ◽  
R Coleman ◽  
M Narasimhan ◽  
D de Mendoza ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site ◽  
Active Site Residues

scholarly journals Amino acid sequence of the active site of Acanthamoeba myosin II.

1986 ◽  
Vol 261 (4) ◽  
pp. 1844-1848
Author(s):  
M A Atkinson ◽  
E A Robinson ◽  
E Appella ◽  
E D Korn
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site ◽  
Myosin Ii

scholarly journals SYNTHESIS AND ANTIMICROBIAL EVALUATION OF QUINAZOLINONE PEPTIDE DERIVATIVES

2017 ◽  
Vol 10 (16) ◽  
pp. 7 ◽  
Author(s):  
Bhupinder Kapoor ◽  
Arshid Nabi ◽  
Reena Gupta ◽  
Mukta Gupta
Keyword(s):  
Antibacterial Activity ◽  
Amino Acid ◽  
Antimicrobial Agents ◽  
Methyl Esters ◽  
Standard Drug ◽  
Amino Acid Peptide ◽  
Chemical Structures ◽  
1H Nuclear Magnetic Resonance ◽  
Peptide Derivatives ◽  
Derivatives Of

  Objective: The increased microbial resistance against commercially available drugs initiated the development of novel and safe antimicrobial agents in last few decades. In this view, a series of amino acid/dipeptide derivatives of quinazolin-3(4H)-one was synthesized and was evaluated for their antimicrobial potential.Method: Synthesis of amino acid/peptide derivatives were carried out by coupling 5-(2-(2-chlorophenyl)-4-oxoquinazolin-3(4H)-yl)-2-hydroxy benzoic acid with amino acid/dipeptide methyl esters in the presence of dicyclohexylcarbodiimide and N-methylmorpholine. The chemical structures of synthesized compounds were characterized by 1H nuclear magnetic resonance and infrared spectroscopy and were screened for antibacterial activity by disc diffusion method.Results: All the synthesized derivatives exhibited moderate to significant antibacterial activity against both Gram-positive and Gram-negative bacteria. The potency of compound 5d was comparable to standard drug ciprofloxacin in all the strains of bacteria used. The compound 5a was found to be more active against Streptococcus pyogenes and Staphylococcus aureus while compound 5c against Pseudomonas aeruginosa and Escherichia coli. Conclusion: Peptide derivatives of quinazolinone are promising antimicrobial agent and can be used for the synthesis of other novel compounds.

Glutamine active site of formylglycinamide ribonucleotide amidotransferase. 2. Amino acid sequence of labeled peptides

Biochemistry ◽  
1977 ◽  
Vol 16 (6) ◽  
pp. 1070-1076 ◽  
Author(s):  
Shiro Ohnoki ◽  
Bor-Shyue Hong ◽  
John M. Buchanan
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site

scholarly journals New class of sensitive and selective fluorogenic substrates for serine proteinases. Amino acid and dipeptide derivatives of rhodamine

1983 ◽  
Vol 215 (2) ◽  
pp. 253-260 ◽  
Author(s):  
S P Leytus ◽  
W L Patterson ◽  
W F Mangel
Keyword(s):  
Amino Acid ◽  
Kinetic Constants ◽  
Amide Bond ◽  
Single Amino Acid ◽  
Amino Acid Derivative ◽  
Specific Substrate ◽  
Serine Proteinases ◽  
Bovine Trypsin ◽  
Human Thrombin ◽  
Derivatives Of

A series of dipeptide derivatives of Rhodamine, each containing an arginine residue in the P1 position and one of ten representative benzyloxycarbonyl (Cbz)-blocked amino acids in the P2 position, has been synthesized, purified and characterized as substrates for serine proteinases. These substrates are easily prepared with high yields. Cleavage of a single amide bond converts the non-fluorescent bisamide substrate into a highly fluorescent monoamide product. Macroscopic kinetic constants for the interaction of these substrates with bovine trypsin, human and dog plasmin, and human thrombin are reported. Certain of these substrates exhibit extremely large specificity constants. For example, the kcat./Km for bovine trypsin with bis-(N-benzyloxycarbonylglycyl-argininamido)-Rhodamine [(Cbz-Gly-Arg-NH)2-Rhodamine] is 1 670 000 M-1 X S-1. Certain of these substrates are also highly selective. For example, the most specific substrate for human plasmin, (Cbz-Phe-Arg-NH2)-Rhodamine, is not hydrolysed by human thrombin, and the most specific substrate for human thrombin, (Cbz-Pro-Arg-NH)2-Rhodamine, is one of the least specific substrates for human plasmin. Comparison of the kinetic constants for hydrolysis of the dipeptide substrates with that of the single amino acid derivative, (Cbz-Arg-NH)2-Rhodamine, indicates that selection of the proper amino acid residue in the P2 position can effect large increases in substrate specificity. This occurs primarily as a result of an increase in kcat. as opposed to a decrease in Km and, in certain cases, is accompanied by a large increase in selectivity. Because of their high degree of sensitivity and selectivity, these Rhodamine-based dipeptide compounds should be extremely useful substrates for studying serine proteinases.

Immunosuppressive properties of amino acid and peptide derivatives of mycophenolic acid

2020 ◽  
Vol 189 ◽  
pp. 112091
Author(s):  
Agnieszka Siebert ◽  
Grzegorz Cholewiński ◽  
Piotr Trzonkowski ◽  
Janusz Rachon
Keyword(s):  
Amino Acid ◽  
Mycophenolic Acid ◽  
Peptide Derivatives ◽  
Derivatives Of

scholarly journals Amino Acid and Peptide Derivatives of Kojic Acid and Their Antifungal Properties

1990 ◽  
Vol 54 (9) ◽  
pp. 2441-2442
Author(s):  
Hiroshi Kayahara ◽  
Norihisa Shibata ◽  
Koji Tadasa ◽  
Hideo Maeda ◽  
Takashi Kotani ◽  
...  
Keyword(s):  
Amino Acid ◽  
Kojic Acid ◽  
Antifungal Properties ◽  
Peptide Derivatives ◽  
Derivatives Of

Synthesis and Antimicrobial and Toxicological Studies of Amino Acid and Peptide Derivatives of Kanamycin A and Netilmicin

1995 ◽  
Vol 38 (23) ◽  
pp. 4710-4719 ◽  
Author(s):  
S. Kotretsou ◽  
M. P. Mingeot-Leclercq ◽  
V. Constantinou-Kokotou ◽  
R. Brasseur ◽  
M. P. Georgiadis ◽  
...  
Keyword(s):  
Amino Acid ◽  
Toxicological Studies ◽  
Peptide Derivatives ◽  
Derivatives Of
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