AI Article Synopsis
- - The study explores how graphene oxide (GO) interacts with important biomolecules, such as certain amino acids and proteins, affecting fluorescence properties and indicating GO's role as a universal quencher for related biomolecules.
- - Fluorescence quenching was found to result mainly from static quenching, with some contribution from dynamic quenching mechanisms, highlighting the complexity of interactions based on conditions like pH.
- - Hydrophobic interactions played a significant role in the quenching process, as demonstrated by the presence of a nonionic copolymer (PF127), which reduced the interaction efficiency between GO and the biomolecules by blocking hydrophobic contact.
Article Abstract
Understanding the interaction between graphene oxide (GO) and the biomolecules is fundamentally essential, especially for disease- and drug-related peptides and proteins. In this study, GO was found to strongly interact with amino acids (tryptophan and tyrosine), peptides (Alzheimer's disease related amyloid beta 1-40 and type 2 diabetes related human islet amyloid polypeptide), and proteins (drug-related bovine and human serum albumin) by fluorescence quenching, indicating GO was a universal quencher for tryptophan or tyrosine related peptides and proteins. The quenching mechanism between GO and tryptophan (Trp) or tyrosine (Tyr) was determined as mainly static quenching, combined with dynamic quenching (Förster resonance energy transfer). Different quenching efficiency between GO and Trp or Tyr at different pHs indicated the importance of electrostatic interaction during quenching. Hydrophobic interaction also participated in quenching, which was proved by the presence of nonionic amphiphilic copolymer Pluronic F127 (PF127) in GO dispersion. The strong hydrophobic interaction between GO and PF127 efficiently blocked the hydrophobic interaction between GO and Trp or Tyr, lowering the quenching efficiency.
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| http://dx.doi.org/10.1021/am302704a | DOI Listing |
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