Temperature manipulating peptide self-assembly in
water nanofilm??
HOU Jia-Hua(侯嘉骅),1DU Qi-Qi-Ge(杜其其格),1 ZHONG Rui-Bo(钟睿博),1ZHANG Ping(张萍),1and ZHANG Feng(张峰)1,?【期刊名称】核技术（英文版）【年(卷),期】2014(025)006【总页数】6
【关键词】Keywords:Peptide self-assembly,Water nanofilm,Microcontact printing,Nanofilament,Hydrohpobicity
Peptide GAV-9 is derived from 3 different disease related proteins.The self-assembly of GAV-9 in a water nanofilm attracted much attention recently.We studied how the temperature factor influenced the peptide selfassembly in a water nanofilm and found interesting phenomena:1)the higher the temperature,the faster the nanofilaments grow;2)the GAV-9 peptide formed double monolayers in a water nanofilm at 60?C,which further supports the hypothesis that the water nanofilm could change the hydrophobicity of mica.We believe these results can help not only the microcontact printing of amyloid peptides,but also a better understanding on how temperature controls the properties of water nanofilm.
I.INTRODUCTION
Amyloid diseases,such as Parkinson disease,Alzheimer’s disease,Creutzfeldt-Jakob disease,Type II Diabetes,often refer to insoluble misfolded protein forming fibrils and their depositing inside cells,which eventually leads to cell death and related function loss[1–4].By studying the fibrillization process of amyloid proteins and their conserved peptide sequences,it is believed that the pathogenic mechanism of these kind of diseases could be understood better[5–9].
We previously synthesized a shortpeptide termed GAV-9(NH2-VGGAVVAGV-CONH2)[10]by comparing the core/conserved sequences of three amyloid
proteins:αsynuclein[11–18],A-β[19–24],and prion proteins[25–28]. By using in situ liquid atomic force microscopy(AFM)imaging,we revealed the different self-assembling manners of GAV-9 in a bulk solution with the help of inorganic templates. On a hydrophilic mica
Temperature manipulating peptide self-assembly in water nanofilm
