On the limited recognition of inorganic surfaces by short peptides compared with antibodies

Abstract

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.

Affinity and Selectivity of Peptides for Inorganic Materials: A Thermodynamic Discussion of the Role of Conformational Flexibility

“…In the latter case, they compared biocombinatorial selection of antibodies and peptides for various GaAs surfaces and found no selective peptide, but they found selective antibodies. 14 The presented minimal model shows that rigid polypeptides always have an edge on flexible ones when they share the same relative mismatch and the same E int , which is in broad agreement with the results of Ref.…”

Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis

“…Recent comparison between free peptide binders and antibody recognition of specic crystal planes shows that a protein-constrained binding loop has greater potential for discriminating between rigid material surface than a exible peptide due to its xed spatial structure and molecular rigidity. 42 This is supported by other studies which indicate that a peptide will be interact with a material differently depending if it is free and exible or constrained into a cyclic structure. 25 The magnetite selected Adhirons appear to have a clear interaction with magnetite nanoparticles in our QCM experiments, conrming that material binding is not dependent upon the presence of the pIII fusion protein, and is not an interaction with the scaffold itself, but a property derived from the variable loops.…”

“…Recent comparison between free peptide binders and antibody recognition of specific crystal planes shows that a protein-constrained binding loop has greater potential for discriminating between rigid material surface than a flexible peptide due to its fixed spatial structure and molecular rigidity. 42 This is supported by other studies which indicate that a peptide will be interact with a material differently depending if it is free and flexible or constrained into a cyclic structure. 25 …”

Designing Fluorescent Peptide Sensors with Dual Specificity for the Detection of HIV-1 Protease

“…Peptides found through phage display are well-known for displaying low to moderate binding affinity. (15)…”

“…Phage display is a powerful technique to identify peptide sequences which show an affinity for a particular target. While it has been most successful in identifying sequences which bind inorganic surfaces, it has also been heavily utilized to identify sequences that can have applications in drug discovery and toward the design of synthetic antibody libraries . Phage-display derived peptides have also successfully been used as biorecognition elements in biosensors …”