Ultrasound-facilitated assembly and disassembly of a pH-sensitive self-assembly peptide

作者: Rong Ni , Jianhui Liu , Ying Chau

DOI: 10.1039/C8RA04391D

关键词: PhenylalanineHistidinePeptideHistidine residueUltrasoundSonicationSelf-assemblyChemistryKineticsBiophysics

摘要: In this report, we investigated the impact of external stimulus (ultrasound) and internal (pH) on peptide assembly disassembly. Two short rationally designed peptides K3C6SPD F20H differing in presence a single pH-sensitive histidine residue were studied as model peptides. The kinetics studies demonstrated that substitution phenylalanine with (F20H) significantly slowed down rate at all three tested pHs (pH 9.5, pH 7.4 5.0). At same time, F to H led increased pH-responsive kinetics. By treating sample beginning process 9.5 for 5 min ultrasound power 2.1 W cm−2, was accelerated lag phase being shortened from 10 days 2 days. For disassembly nanofibrils preformed upon adjustment 5.0, ultrasonication resulted nanofibril within 6 hours, instead absence ultrasound. On contrary, similar treatment did not produce any obvious effect both processes. This study offers an effective strategy modulate stimuli-responsiveness peptide-based biomaterials.

参考文章(27)
Yuji Goto, Seung R Paik, Eri Chatani, Hyun Jin Kim, Seed-dependent accelerated fibrillation of alpha-synuclein induced by periodic ultrasonication treatment. Journal of Microbiology and Biotechnology. ,vol. 17, pp. 2027- 2032 ,(2007)
Ehud Gazit, A possible role for π-stacking in the self-assembly of amyloid fibrils The FASEB Journal. ,vol. 16, pp. 77- 83 ,(2002) , 10.1096/FJ.01-0442HYP
Risto Cukalevski, Barry Boland, Birgitta Frohm, Eva Thulin, Dominic Walsh, Sara Linse, Role of aromatic side chains in amyloid β-protein aggregation. ACS Chemical Neuroscience. ,vol. 3, pp. 1008- 1016 ,(2012) , 10.1021/CN300073S
Thomas J. Measey, Feng Gai, Light-triggered disassembly of amyloid fibrils. Langmuir. ,vol. 28, pp. 12588- 12592 ,(2012) , 10.1021/LA302626D
Kentaro Uesugi, Hirotsugu Ogi, Masahiko Fukushima, Masatomo So, Hisashi Yagi, Yuji Goto, Masahiko Hirao, Mechanisms of Ultrasonically Induced Fibrillation of Amyloid β1–40Peptides Japanese Journal of Applied Physics. ,vol. 52, pp. 07HE10- ,(2013) , 10.7567/JJAP.52.07HE10
Charalampos G. Pappas, Tapiwa Mutasa, Pim W. J. M. Frederix, Scott Fleming, Shuo Bai, Sisir Debnath, Sharon M. Kelly, Anthony Gachagan, Rein V. Ulijn, Transient supramolecular reconfiguration of peptide nanostructures using ultrasound Materials horizons. ,vol. 2, pp. 198- 202 ,(2015) , 10.1039/C4MH00223G
Sibaprasad Maity, Pankaj Kumar, Debasish Haldar, Sonication-induced instant amyloid-like fibril formation and organogelation by a tripeptide Soft Matter. ,vol. 7, pp. 5239- 5245 ,(2011) , 10.1039/C1SM05277B
H. Yokoi, T. Kinoshita, S. Zhang, Dynamic reassembly of peptide RADA16 nanofiber scaffold Proceedings of the National Academy of Sciences of the United States of America. ,vol. 102, pp. 8414- 8419 ,(2005) , 10.1073/PNAS.0407843102
Connie S. Kwok, Pierre D. Mourad, Lawrence A. Crum, Buddy D. Ratner, Self-assembled molecular structures as ultrasonically-responsive barrier membranes for pulsatile drug delivery. Journal of Biomedical Materials Research. ,vol. 57, pp. 151- 164 ,(2001) , 10.1002/1097-4636(200111)57:2<151::AID-JBM1154>3.0.CO;2-5
Yong-Bo Hu, Eric B Dammer, Ru-Jing Ren, Gang Wang, The endosomal-lysosomal system: from acidification and cargo sorting to neurodegeneration. Translational neurodegeneration. ,vol. 4, pp. 18- 18 ,(2015) , 10.1186/S40035-015-0041-1