作者: Tungalag Battulga , Oyunjargal Tumurbaatar , Oyundelger Ganzorig , Takahisa Ishimura , Taisei Kanamoto
DOI: 10.1016/J.IJBIOMAC.2018.12.010
关键词: Oligopeptide 、 Surface plasmon resonance 、 Curdlan 、 Peptide 、 Lysine 、 Sulfation 、 Molecular mass 、 Amino acid 、 Chemistry 、 Stereochemistry
摘要: Abstract This study aims to quantitatively investigate the interaction between sulfated polysaccharides with potent anti-HIV activity, dextran and curdlan sulfates negatively charged sulfate groups, poly- L -lysine as a model protein oligopeptides from HIV surface glycoprotein gp120 positively amino acids using plasmon resonance (SPR) dynamic light scattering (DLS) elucidate mechanism of polysaccharides. The apparent association- (ka) dissociation rate (kd) constants against were ka = 6.92 × 104–2.17 × 106 1/Ms kd = 4.29 × 10−5–2.22 × 10−4 1/s; these kinetic dependent on molecular weights degree sulfation For interaction, three peptide A 297T R PNNNT RKR I IQ GPG A316 several lysine (K) arginine (R) in V3 loop region, B 493PLGVAPT K KRR VVQ E KR 511 C-terminus oligopeptide C 362 QSSGGDPEIVTHSFNCGG380 few basic CD4 binding domain. Sulfated exhibited strong B, (ka = 5.48 × 104–2.96 × 106 1/Ms. kd = 1.74 × 10−4–6.24 × 10−3 1/s), no was noted C. Moreover, particle size zeta potential by DLS indicated suggesting be electrostatic at acid regions.