Binding Specificity of a Peptide on Semiconductor Surfaces

Binding Specificity of a Peptide on Semiconductor Surfaces
复制标题

DOI:
10.1021/nl048829p
复制
发表时间:
2004-09
期刊:
影响因子:
10.8
通讯作者:
K. Goede;P. Busch;M. Grundmann
K. Goede;P. Busch;M. Grundmann
中科院分区:
材料科学1区
文献类型:
--
作者:
K. Goede;P. Busch;M. Grundmann

文献摘要

被引文献

相似文献

用原子力显微镜定量研究了多肽在半导体表面的粘附性。可重复地发现所选的12聚体多肽以底物特异性的方式附着在各种III、−、V和IV族半导体表面。观察到的Al0.98Ga0.02As、Si、Ge、InP、GAP、GaP、GaP、GaP的多肽附着系数的递增是由底物电负性和氨基酸侧链的酸性定性地解释的。结果表明,多肽的粘附性强烈依赖于氨基酸序列。
Peptide adhesion on semiconductors is quantitatively investigated by atomic force microscopy. A selected 12-mer peptide is reproducibly found to adhere to various III−V and group-IV semiconductor surfaces in a substrate-specific way. The observed succession Al0.98Ga0.02As, Si, Ge, InP, GaP, GaAs in terms of increasing peptide adhesion coefficients is qualitatively explained by the substrate electronegativity and the acidity of the amino acid side chains. It is shown that peptide adhesion is strongly dependent on the amino acid sequence.