Constructing biomaterials using self-assembling peptide building blocks

Lu, Shan; Chen, P.

doi:10.1007/s11706-010-0021-4

Cited by 6 publications

(1 citation statement)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Characteristic properties of amino acids, such as responsiveness, chemical and biological modularity, and recognition by living organisms make peptide-based systems indispensable tools for medical purposes. Among the medical application areas some of the most important are tissue engineering, regenerative medicine, gene and drug delivery, , biosensors, , and hydrogels. − A key requirement for many of these application areas is that these molecules should exhibit a well-defined and stable equilibrium conformation under stringent conditions and self-assemble to enable bottom-up design strategies. ,,− …”

Section: Introductionmentioning

confidence: 99%

Adsorption, Folding, and Packing of an Amphiphilic Peptide at the Air/Water Interface

Engin

Sayar

2012

J. Phys. Chem. B

View full text Add to dashboard Cite

Peptide oligomers play an essential role as model compounds for identifying key motifs in protein structure formation and protein aggregation. Here, we present our results, based on extensive molecular dynamics simulations, on adsorption, folding, and packing within a surface monolayer of an amphiphilic peptide at the air/water interface. Experimental results suggest that these molecules spontaneously form ordered monolayers at the interface, adopting a β-hairpin-like structure within the surface layer. Our results reveal that the β-hairpin structure can be observed both in bulk and at the air/water interface. However, the presence of an interface leads to ideal partitioning of the hydrophobic and hydrophilic residues, and therefore reduces the conformational space for the molecule and increases the stability of the hairpin structure. We obtained the adsorption free energy of a single β-hairpin at the air/water interface, and analyzed the enthalpic and entropic contributions. The adsorption process is favored by two main factors: (1) Free-energy reduction due to desolvation of the hydrophobic side chains of the peptide and release of the water molecules which form a cage around these hydrophobic groups in bulk water. (2) Reduction of the total air/water contact area at the interface upon adsorption of the peptide amphiphile. By performing mutations on the original molecule, we demonstrated the relative role of key design features of the peptide. Finally, by analyzing the potential of mean force among two peptides at the interface, we investigated possible packing mechanisms for these molecules within the surface monolayer.

show abstract