CHARACTERIZATION OF PEPTIDE-SURFACE INTERACTIONS

生物分子与表面的相互作用对于生物活性剂的功效至关重要。 生物分析分离、生物传感器和假体装置。 尽管 他们的重要性，很少有人知道基本化学和 生物分子和表面之间的物理相互作用。 的目标 拟议的研究是表征非共价相互作用的 肽与金属表面。 该提案描述了系统的研究 旨在确定特定的官能团和构象 氨基酸、肽和小多肽中的限制控制着 这些生物分子的吸附、取向和表面相互作用。 这些结果将大大扩展我们对肽金属的理解 相互作用，以及我们对吸附行为的理解， 在溶液-固体界面处的多官能分子。 肽是蛋白质的优良化学和光谱模型。 我们 因此，将使用肽来确定 特定的官能团和构象限制， 肽和蛋白质的吸收率和表面相互作用， 非反应性表面。 用于非共价吸附物表面的研究 所有基质都有共同的相互作用，贵金属几乎 理想的模型表面。 它们的表面化学成分相对简单 与石英、二氧化硅和聚合物相比。 表面净电荷 并且疏水性可以简单地通过改变所施加的电势来改变， 支持电解质和金属本身。 这些研究中使用的主要工具是拉曼和红外 光谱学，特别强调表面增强拉曼 由于其独特的灵敏度和选择性， 吸附在贵金属表面上。 我们的初步Sers结果 证明了这种方法的可行性，并揭示了肽 吸收受特定官能团-表面相互作用的控制 规定了溶液中吸附物的方向和构象 金属界面 特别是，结果表明，肽相互作用 与银通过末端胺基和通过芳族 侧链，特别是酪氨酸，在拟议的工作中，我们将 表征这些和其他肽官能团-表面相互作用 并评估它们对肽相对贡献 吸收率 第二个目标是确定表面 电荷、疏水性和粗糙度影响肽和多肽 吸附作用

Biomolecule-surface interactions are essential to the efficacy of bioanalytical separations, biosensors, and prosthetic devices. Despite their importance, very little is known about fundamental chemical and physical interactions between biomolecules and surfaces. The goal of the proposed research is to characterize the non-covalent interactions of peptides with metal surfaces. This proposal describes systematic studies aimed at determining how specific functional groups and conformational constraints in amino acids, peptides, and small polypeptides control the adsorption, orientation, and surface interactions of these biomolecules. The results will significantly extend our understanding of peptide-metal interactions, and our understanding of the adsorption behavior of polyfunctional molecules at solution-solid interfaces. Peptides are excellent chemical and spectroscopic models for proteins. We will therefore use peptides to determine the relative importance of specific functional groups and conformational constraints in determining the absorptivity and surface interactions of peptides and proteins with non-reactive surfaces. For studies of the non-covalent adsorbate-surface interactions that are common to all substrates, noble metals are nearly ideal model surfaces. Their surface chemistry is relatively simple compared with that of quartz, silica, and polymers. The net surface charge and hydrophobicity can be varied simply by changing the applied potential, the supporting electrolyte, and the metal itself. The primary tools that will be used in these studies are Raman and infrared spectroscopy, with particular emphasis on surface-enhanced Raman spectroscopy (SERS) because of its unique sensitivity and selectivity for adsorbates on noble metal surfaces. Our preliminary SERS results demonstrate the feasibility of this approach, and reveal that peptide absorption is governed by specific functional group-surface interactions that prescribe the adsorbate orientation and conformation at the solution- metal interface. In particular, the results suggest that peptides interact strongly with silver through the terminal amine group and through aromatic side chains, particularly tyrosine, In the proposed work we will characterize these and other peptide functional group-surface interactions in detail, and evaluate their relative contributions to peptide absorptivity. A secondary objective is to determine how the surface charge, hydrophobicity, and roughness affect peptide and polypeptide adsorption.