Design of Common Bean Lectin Inhibitor and Its Hemagglutination Activity†

doi:10.7503/cjcu20170064

Abstract

Abstract:

Common bean(Phaseolus vulgaris L.), rich in protein and low in fat, is one of the most important legume crops in the world. However, consumption of improperly prepared common bean can lead to food poisoning. Previous studies have largely attributed this toxic effect to the high content in lectin, a plant protein that binds specifically to carbohydrate or carbohydrate structures displayed on cell surface. Since most lectin forms a dimer complex for biological functions, a short peptide was designed to break the dimer interface. Detailed dynamical network and structural characteristic analysis were performed to select this peptide. In vitro hemagglutination assay showed that this peptide, upon binding to lectin, disrupts the dimer formation partially and weakens the hemagglutination effect. Taken together, a novel peptide inhibitor was designed whose potency and specificity can be further optimized for anti-hemagglutination and food safety applications.

Key words: Common bean lectin, Molecular dynamics simulation, Drug design, Inhibitor design, Hemagglutination activity

CLC Number:

O629.7

TrendMD:

LIU Qin, YU Yanhua, CHEN Weida, CHEN Chanyou, ZHAO Yunjie, ZENG Chen. Design of Common Bean Lectin Inhibitor and Its Hemagglutination Activity^†[J]. Chem. J. Chinese Universities, 2017, 38(7): 1185.

Figures/Tables 5

Fig.1 Structural analysis of common bean lectin dimer structure(A) Common bean lectin dimer structure(PDB code: 3WCR, chain A, chain B, β strand and NAG are colored in green, cyan, red and magenta, respectively); (B) β strand interface structure(GLU182-ASP217, less conserved or variable residues are colored in blue).

Table 1 Conservation analysis of the common bean lectin dimer interface residues

Position	Residue	Conservation	Position	Residue	Conservation	Position	Residue	Conservation
182	GLU	3	194	THR	7	206	LEU	2
183	ASN	5	195	LYS	6	207	LYS	2
184	ALA	7	196	LEU	5	208	THR	6
185	GLU	5	197	LEU	8	209	SER	6
186	VAL	8	198	VAL	7	210	PHE	4
187	LEU	3	199	ALA	8	211	ILE	6
188	ILE	9	200	SER	6	212	VAL	5
189	THR	6	201	LEU	7	213	SER	7
190	TYR	9	202	VAL	5	214	ASP	3
191	ASP	6	203	TYR	5	215	THR	4
192	SER	7	204	PRO	4	216	VAL	8
193	SER	5	205	SER	6	217	ASP	8

Fig.2 Dynamic correlation analysis of the interface residues(GLU182-ASP217) between two monomers

Fig.3 Potential binding pocket at the interface for inhibitor designPDB code: 3WCR, chain A, chain B and pocket are colored in green, cyan and red, respectively.

Fig.4 Inhibitory effect of the peptide in hemagglutination assay

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