Attenuating HIV Tat/TAR-mediated protein expression by exploring the side chain length of positively charged residues

2015 ◽  
Vol 13 (45) ◽  
pp. 11096-11104 ◽  
Author(s):  
Cheng-Hsun Wu ◽  
Yi-Ping Chen ◽  
Shing-Lung Liu ◽  
Fan-Ching Chien ◽  
Chung-Yuan Mou ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Expression ◽  
Chain Length ◽  
Protein Production ◽  
Side Chain ◽  
Amino Acid Side Chain ◽  
Intracellular Protein ◽  
Hiv Tat ◽  
Chain Lengths ◽  
Positively Charged

Altering amino acid side chain lengths enhanced multiple bioactivities and inhibited intracellular protein production.

Effect of charged amino acid side chain length on lateral cross-strand interactions between carboxylate- and guanidinium-containing residues in a β-hairpin

Amino Acids ◽  
2015 ◽  
Vol 47 (5) ◽  
pp. 885-898 ◽  
Author(s):  
Hsiou-Ting Kuo ◽  
Shing-Lung Liu ◽  
Wen-Chieh Chiu ◽  
Chun-Jen Fang ◽  
Hsien-Chen Chang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Chain Length ◽  
Side Chain ◽  
Amino Acid Side Chain ◽  
Side Chain Length

scholarly journals Chain Length of Amphipathic-Type Thioesters Dramatically Affects Reactivity in Aqueous Amidation Reactions with Cysteine Esters

SynOpen ◽  
2017 ◽  
Vol 01 (01) ◽  
pp. 0059-0062
Author(s):  
Ikumi Otomo ◽  
Kanna Watanabe ◽  
Chiaki Kuroda ◽  
Kenichi Kobayashi
Keyword(s):  
Amino Acid ◽  
Aqueous Medium ◽  
Chain Length ◽  
Ethyl Esters ◽  
Side Chain ◽  
Amino Acid Side Chain ◽  
Hydrophobic Properties ◽  
M 10 ◽  
Hexyl Ester ◽  
Close Proximity

The reaction of five amphipathic-type thioesters, CH3(CH2) m COS(CH2) n COONa (m + n = 12), with cysteine hexyl, butyl, and ethyl esters were studied in aqueous medium. Compounds with the thioester group in close proximity to the carboxylate moiety (m = 10, n = 2) afforded amides in almost quantitative yield, whereas no reaction proceeded by using compounds with the thioester group distant from the carboxylate. In contrast, no clear difference in yield was observed among the five amphipathic-type thioesters upon reaction with valine hexyl ester. The results indicate that the reaction is affected by both the position of the thioester group and the hydrophilic/hydrophobic properties of the amino acid side chain.

Effect of Charged Amino Acid Side Chain Length at Non-Hydrogen Bonded Strand Positions on β-Hairpin Stability

Biochemistry ◽  
2013 ◽  
Vol 52 (44) ◽  
pp. 7785-7797 ◽  
Author(s):  
Li-Hung Kuo ◽  
Jhe-Hao Li ◽  
Hsiou-Ting Kuo ◽  
Cheng-Yun Hung ◽  
Hsin-Yun Tsai ◽  
...  
Keyword(s):  
Amino Acid ◽  
Chain Length ◽  
Side Chain ◽  
Amino Acid Side Chain ◽  
Side Chain Length ◽  
Hydrogen Bonded

Effect of the basic amino-acid side chain length and the penultimate residue on the hydrolysis of benzoyldipeptides by carboxypeptidase B

1978 ◽  
Vol 56 (5) ◽  
pp. 315-318 ◽  
Author(s):  
Graham J. Moore ◽  
N. Leo Benoiton
Keyword(s):  
Amino Acid ◽  
Chain Length ◽  
Basic Amino Acid ◽  
Side Chain ◽  
Amino Acid Side Chain ◽  
Carboxypeptidase B ◽  
Side Chain Length ◽  
C Terminus ◽  
Guanidino Group ◽  
Hydrolysis Of

The kinetic parameters Km and kcat/Km have been determined for the carboxypeptidase B (CPB, EC 3.4.12.3) catalyzed hydrolysis of benzoylglycyl-DL-homolysine and benzoylglycyl-L-homoarginine. Plots of these data and those for Bz-Gly-Orn and Bz-Gly-Arg (Wolff, E. C., Schirmer, E. W. &Folk, J. E. (1962) J. Biol. Chem. 237, 3094–3099) and Bz-Gly-Lys versus the length of the side chain of the basic amino acid indicate that unlike trypsin (EC 3.4.21.4) (Seely, J. H. &Benoiton, N. L. (1970) Can. J. Biochem. 48, 1122–1131) CPB has a higher binding affinity for a guanidino group than for an amino group at the side chain of the substrate C-terminus. On the other hand, CPB is similar to trypsin (ibid) in that the best substrate would have a side chain length between those of lysine and arginine.Studies with Bz-MeGly-Lys and Bz-Ala-Lys showed that the former is very slowly hydrolyzed by CPB but that the latter is a good substrate, with a high affinity for the enzyme, indicative of considerable participation of the Cα-methyl group of alanine in the binding of the substrate to the enzyme.

Exploring the impact of the side-chain length on peptide/RNA binding events

2017 ◽  
Vol 19 (28) ◽  
pp. 18452-18460
Author(s):  
Lola Sbicca ◽  
Alejandro López González ◽  
Alexandra Gresika ◽  
Audrey Di Giorgio ◽  
Jordi Teixido Closa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Chain Length ◽  
Rna Binding ◽  
Side Chain ◽  
Amino Acid Side Chain ◽  
Side Chain Length ◽  
Tar Rna ◽  
The Impact ◽  
Hiv 1

The impact of the amino-acid side-chain length on peptide–RNA binding events has been investigated using HIV-1 Tat derived peptides as ligands and the HIV-1 TAR RNA element as an RNA model.

Investigating peptide sequence variations for ‘double-click’ stapled p53 peptides

2014 ◽  
Vol 12 (24) ◽  
pp. 4074-4077 ◽  
Author(s):  
Yu Heng Lau ◽  
Peterson de Andrade ◽  
Niklas Sköld ◽  
Grahame J. McKenzie ◽  
Ashok R. Venkitaraman ◽  
...  
Keyword(s):  
Amino Acid ◽  
Point Mutation ◽  
Chain Length ◽  
Peptide Sequence ◽  
Side Chain ◽  
Amino Acid Side Chain ◽  
Side Chain Length ◽  
Sequence Variations ◽  
P53 Peptides

Evaluating the influence of staple position, azido amino acid side-chain length and point mutation on the activity of ‘double-click’ stapled p53 peptides.

Effect of Charged Amino Acid Side Chain Length on Lateral Cross-Strand Interactions between Carboxylate-Containing Residues and Lysine Analogues in a β-Hairpin

Biochemistry ◽  
2013 ◽  
Vol 52 (51) ◽  
pp. 9212-9222 ◽  
Author(s):  
Hsiou-Ting Kuo ◽  
Chun-Jen Fang ◽  
Hsin-Yun Tsai ◽  
Min-Fan Yang ◽  
Hsien-Chen Chang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Chain Length ◽  
Side Chain ◽  
Amino Acid Side Chain ◽  
Side Chain Length

Amino acid side-chain populations in aqueous and saline solution: Bis-penicillamine enkephalin

Biopolymers ◽  
1992 ◽  
Vol 32 (12) ◽  
pp. 1623-1629 ◽  
Author(s):  
Paul E. Smith ◽  
B. Montgomery Pettitt
Keyword(s):  
Amino Acid ◽  
Saline Solution ◽  
Side Chain ◽  
Amino Acid Side Chain
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