Interactions of carrageenan or its degradation product with R15K by affinity capillary electrophoresis

doi:10.5246/jcps.2015.06.051

Abstract

Abstract:

V3 loop of HIV-1 envelop protein gp120 plays a pivotal role in the entry process of HIV-1 into target cells. R15K, the relatively conserved region of V3 loop, can be used in binding studies instead of recombinant gp120 molecule. Polyanionic compounds, such as carrageenan, possess antiviral activity through disrupting gp120-CD4 interaction, and chemical modifications have been performed to improve such activity. In this work, we, for the first time, analyzed the interactions between carrageenan or its degradation and R15K by affinity capillary electrophoresis (ACE). Our results revealed that depolymerized carrageenan rather than carrageenan could bind to R15K. The binding constant of depolymerized carrageenan was (2.94±0.57)×10⁶mol/L. Our finding indicated that the depolymerized carrageenan could be R15K antagonist, and it might inhibit the infection of HIV-1 through the entry process.

Key words: HIV-1, V3 peptides, ACE, Carrageenan, Carrageenan degradation

CLC Number:

R917

Supporting:

Zhongjie Li, Li Li, Xiaowei Wang, Junyi Liu, Xiaomei Ling. Interactions of carrageenan or its degradation product with R15K by affinity capillary electrophoresis[J]. Journal of Chinese Pharmaceutical Sciences, 2015, 24(6): 400-404.

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