Self-assembling bolaamphiphile-like collagen mimetic peptides

Abstract

Bolaamphiphile-like collagen mimetic peptides with charged aspartic acids at both terminals may provide a facile peptide-based approach to construct well-defined nanostructures.

Promotion of the collagen triple helix in a hydrophobic environment

“…In this context, a notable observation was recently reported by Yao et al: they have demonstrated that the addition of polar terminal residues to the CMP scaffold promotes their assembly into a separate phase in water, thereby forming nanospherical particles. 25,26 As the conclusion from our literature survey, there is an unfortunate lack of information on whether CMPs would assemble in a hydrophobic environment, and how the triple helix is maintained under non-aqueous conditions. To this end, we decided to design CMPs with an amplified hydrophobicity of the triple helical exterior, with the idea that this would force the peptides to assemble in nonpolar environments.…”

Formation of Microcages from a Collagen Mimetic Peptide via Metal-Ligand Interactions

“…The de novo design of collagen mimetic peptides (CMPs) containing additional higher-order assembly signals allows for the possibility of generating collagen peptide-based materials with morphologies and applications not found for natural collagen [ 9 ]. A variety of chemistries has been used to prompt the assembly of these peptides, such as exploitation of cysteine knots [ 10 , 11 , 12 ], native chemical ligation [ 13 ], electrostatic interactions [ 14 , 15 , 16 , 17 , 18 , 19 ], hydrophobic interactions [ 20 , 21 , 22 ], π-π interactions [ 23 , 24 ], and cation-π interactions [ 25 ].…”

Designing a bioactive scaffold from coassembled collagen–laminin short peptide hydrogels for controlling cell behaviour

“…13,14 The characteristic triple helical structure of collagen is stabilized by the close packing of glycine and hydrogen bond formed between the amide proton of glycine and carbonyl group of nearby Xresidue. 15 A classical report by Ramachandran and co-workers explained the role of hydroxyproline residues in stabilizing the collagen triple helix via additional H-bonding between hydroxyl group of hydroxyproline and water molecules. 16 Further, self-assembly of triple helices provides mechanical strength and structural integrity to the body.…”

“…16 Further, self-assembly of triple helices provides mechanical strength and structural integrity to the body. 15 Crucial advancements have been made in replicating the multi-hierarchical self-assembly of collagen and towards understanding the fundamentals of design of native collagen. To this direction, collagen mimetic peptides (CMP) have been evolved as the potential biomaterial for biomedical applications, like, tissue engineering, drug delivery, diagnostics and therapy, etc.…”

“… 16 Further, self-assembly of triple helices provides mechanical strength and structural integrity to the body. 15 …”