Controlled peptide solvation in portion-mixing libraries of FRET peptides: improved specificity determination for Dengue 2 virus NS2B-NS3 protease and human cathepsin S.

Controlled peptide solvation in portion-mixing libraries of FRET peptides: improved specificity determination for Dengue 2 virus NS2B-NS3 protease and human cathepsin S. Research Abstract Details 

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Controlled peptide solvation in portion-mixing libraries of FRET peptides: improved specificity determination for Dengue 2 virus NS2B-NS3 protease and human cathepsin S. Abstract Text:

Fabiana M Alves,Izaura Y Hirata,Iuri E Gouvea,Marcio F M Alves,Morten Meldal,Dieter ,Luiz Juliano,Maria A Juliano,

The solubility of peptides in aqueous buffers used for the enzyme assays is a common limitation for all peptide libraries. In principle, the more water-soluble peptides are, the more susceptible they will be to peptidase hydrolysis. We have demonstrated that this bias can be circumvented in a portion-mixing fluorescence resonance energy transfer (FRET) peptide library by introducing k (lysine in the D-form) in both termini of the peptides. This more solvated library and another one without the k were assayed using trypsin and chymotrypsin as standard peptidases with high selectivity for R and K and for hydrophobic F and Y, respectively. Significantly improved consistency of the information on substrate profiles was obtained from the solvated library. The influence of improved solvation on substrate specificity determination was successfully demonstrated by the difference in specificity observed between the two libraries employing the human cathepsin S (accepts acidic, basic, or neutral amino acids at P1 position) and Dengue 2 virus NS2B-NS3 protease (high specificity to the pair of basic amino acids K-R, R-R, or Q-R/K at P2-P1 positions). In conclusion, hydration of the peptides has a major influence on protease processing, and this bias can be reduced in bound peptide libraries, improving reliability.

Controlled peptide solvation in portion-mixing libraries of FRET peptides: improved specificity determination for Dengue 2 virus NS2B-NS3 protease and human cathepsin S. Publishing Authors By Initials

FM Alves,IY Hirata,IE Gouvea,MF Alves,M Meldal,D ,L Juliano,MA Juliano,

For similar proteins: viral proteins: viral nonstructural proteins research abstracts see: proteins: viral proteins: viral nonstructural proteins research

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Controlled peptide solvation in portion-mixing libraries of FRET peptides: improved specificity determination for Dengue 2 virus NS2B-NS3 protease and human cathepsin S. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of combinatorial chemistry

VOLUME: 9

Page Numbers: 627-34

Journal Abbreviation:

ISSN: 1520-4766

DAY: 12

MONTH: 06

YEAR: 2007

Controlled peptide solvation in portion-mixing libraries of FRET peptides: improved specificity determination for Dengue 2 virus NS2B-NS3 protease and human cathepsin S. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 100886263

Controlled peptide solvation in portion-mixing libraries of FRET peptides: improved specificity determination for Dengue 2 virus NS2B-NS3 protease and human cathepsin S. Keywords Mesh Terms:

KEYWORDS: Viral Nonstructural Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Controlled peptide solvation in portion-mixing libraries of FRET peptides: improved specificity determination for Dengue 2 virus NS2B-NS3 protease and human cathepsin S. Information

Substance Name: cathepsin S

Registry Number: EC 3.4.22.27

Grant and Affiliation Information for Controlled peptide solvation in portion-mixing libraries of FRET peptides: improved specificity determination for Dengue 2 virus NS2B-NS3 protease and human cathepsin S.

AFFILIATION: Department of Biophysics, Escola Paulista de Medicina, UNIFESP, Rua Três de Maio, 100, São Paulo 04044-020, Brazil.

Country: United States

AGENCY: United States NIAMS

GRANT: AR 48669

ACRONYM: AR

MEDLINETA: J Comb Chem

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