Department of Biology, Technion - Israel Institute of Technology, Haifa, 32000, Israel; Department of Physics, Technion - Israel Institute of Technology, Haifa, 32000, Israel; The Russell Berrie Nanotechnology Institute, Technion - Israel Institute of Technology, Haifa, 32000, Israel.
J Pept Sci. 2014 Jun;20(6):446-50. doi: 10.1002/psc.2636. Epub 2014 Apr 15.
The vast potential applications of biomolecules that bind inorganic surfaces led mostly to the isolation of short peptides that target selectively specific materials. The demonstrated differential affinity toward certain surfaces created the impression that the recognition capacity of short peptides may match that of rigid biomolecules. In the following, we challenge this view by comparing the capacity of antibody molecules to discriminate between the (100) and (111A) facets of a gallium arsenide semiconductor crystal with the capacity of short peptides to do the same. Applying selection from several peptide and single chain phage display libraries, we find a number of antibody molecules that bind preferentially a given crystal facet but fail to isolate, in dozens of attempts, a single peptide capable of such recognition. The experiments underscore the importance of rigidity to the recognition of inorganic flat targets and therefore set limitations on potential applications of short peptides in biomimetics.
生物分子与无机表面结合的广泛潜在应用主要导致了针对特定材料选择性靶向的短肽的分离。对某些表面表现出的差异亲和力给人留下了这样的印象，即短肽的识别能力可能与刚性生物分子相当。在接下来的内容中，我们通过比较抗体分子区分砷化镓半导体晶体的 (100) 和 (111A) 晶面的能力与短肽的区分能力来挑战这一观点。通过对几个肽和单链噬菌体展示文库的选择，我们发现了一些抗体分子，它们优先结合特定的晶体晶面，但在数十次尝试中，都无法分离出能够识别这种晶面的单一肽。这些实验强调了刚性对无机平面靶识别的重要性，因此限制了短肽在仿生学中的潜在应用。
