TY - JOUR
T1 - Molecular self-assembly and applications of designer peptide amphiphiles
AU - Zhao, Xiubo
AU - Pan, Fang
AU - Xu, Hai
AU - Yaseen, Mohammed
AU - Shan, Honghong
AU - Hauser, Charlotte A.E.
AU - Zhang, Shuguang
AU - Lu, Jian R.
PY - 2010/8/18
Y1 - 2010/8/18
N2 - Short synthetic peptide amphiphiles have recently been explored as effective nanobiomaterials in applications ranging from controlled gene and drug release, skin care, nanofabrication, biomineralization, membrane protein stabilization to 3D cell culture and tissue engineering. This range of applications is heavily linked to their unique nanostructures, remarkable simplicity and biocompatibility. Some peptide amphiphiles also possess antimicrobial activities whilst remaining benign to mammalian cells. These attractive features are inherently related to their selective affinity to different membrane interfaces, high capacity for interfacial adsorption, nanostructuring and spontaneous formation of nano-assemblies. Apart from sizes, the primary sequences of short peptides are very diverse as they can be either biomimetic or de novo designed. Thus, their self-assembling mechanistic processes and the nanostructures also vary enormously. This critical review highlights recent advances in studying peptide amphiphiles, focusing on the formation of different nanostructures and their applications in diverse fields. Many interesting features learned from peptide self-organisation and hierarchical templating will serve as useful guidance for functional materials design and nanobiotechnology (123 references).
AB - Short synthetic peptide amphiphiles have recently been explored as effective nanobiomaterials in applications ranging from controlled gene and drug release, skin care, nanofabrication, biomineralization, membrane protein stabilization to 3D cell culture and tissue engineering. This range of applications is heavily linked to their unique nanostructures, remarkable simplicity and biocompatibility. Some peptide amphiphiles also possess antimicrobial activities whilst remaining benign to mammalian cells. These attractive features are inherently related to their selective affinity to different membrane interfaces, high capacity for interfacial adsorption, nanostructuring and spontaneous formation of nano-assemblies. Apart from sizes, the primary sequences of short peptides are very diverse as they can be either biomimetic or de novo designed. Thus, their self-assembling mechanistic processes and the nanostructures also vary enormously. This critical review highlights recent advances in studying peptide amphiphiles, focusing on the formation of different nanostructures and their applications in diverse fields. Many interesting features learned from peptide self-organisation and hierarchical templating will serve as useful guidance for functional materials design and nanobiotechnology (123 references).
UR - http://www.scopus.com/inward/record.url?scp=77955825528&partnerID=8YFLogxK
U2 - 10.1039/b915923c
DO - 10.1039/b915923c
M3 - Article
C2 - 20498896
AN - SCOPUS:77955825528
SN - 0306-0012
VL - 39
SP - 3480
EP - 3498
JO - Chemical Society Reviews
JF - Chemical Society Reviews
IS - 9
ER -