期刊
CHEMISTRY-A EUROPEAN JOURNAL
卷 14, 期 1, 页码 143-150出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.200701234
关键词
chirality; gold; molecular; recognition; nanoparticles; proteins
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM077173] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM077173] Funding Source: Medline
Amino acid and dipeptide-functionalized gold nanoparticles (NPs) possessing L/D-leucine and/or L/D-phenylalanine residues have been constructed in order to target the surfaces of a.-chymotrypsin (ChT) and cytochrome c (CytC). Isothermal titration calorimetry (ITC) was conducted to evaluate the binding thermodynamics and selectivity of these NP-protein interactions. The chirality of the NP end-groups substantially affects the resultant complex stability, with up to 20-fold differences seen between particles of identical hydrophobicity, demonstrating that structural information from the ligands can be used to control protein recognition.
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