Guest-binding behavior of peptide nanocapsules self-assembled from viral peptide fragments
نویسندگان
چکیده
The binding behavior of guests (dyes and DNA) into peptide nanocapsules formed via self-assembly of a 24-mer b-annulus peptide fragment obtained from the capsid protein of the tomato bushy stunt virus is reported. The pH dependence of the f potential of the peptide nanocapsules indicates that the Cand N-termini are directed to the exterior and interior of the nanocapsules, respectively. Equilibrium dialysis experiments with dyes and the peptide nanocapsules at pH 7 showed that the peptide nanocapsules tend to bind anionic dyes. Binding of sodium 8-anilinonaphthalene-1-sulfonate and uranine into the peptide nanocapsules minimally affected the size of the nanocapsules, whereas binding of other anionic dyes resulted in the formation of precipitates. In addition, binding of Thioflavin T to the b-annulus peptide promoted disassembly of the nanocapsules. Complexation of the b-annulus peptide with M13 phage DNA formed a core-shell nanosphere in which the DNA was encapsulated in the peptide assembly. Polymer Journal (2013) 45, 529–534; doi:10.1038/pj.2012.235; published online 23 January 2013
منابع مشابه
Inclusion of Zinc Oxide Nanoparticles into Virus-Like Peptide Nanocapsules Self-Assembled from Viral β-Annulus Peptide
A viral β-annulus peptide connected with a zinc oxide (ZnO)-binding sequence (HCVAHR) at its N-terminal was synthesized, and the inclusion behavior of quantum-sized ZnO nanoparticles into the peptide nanocapsules formed by self-assembly of the peptide in water was investigated. Dynamic light scattering (DLS) measurements showed that ZnO nanoparticles (approximately 10 nm) in the presence of the...
متن کاملBioinspired self-assembled peptide nanofibers with thermostable multivalent α-helices.
The stabilization of peptide's active conformation is a critical determinant of its target binding efficiency. Here we present a structure-based self-assembly strategy for the design of nanostructures with multiple and thermostable α-helices using bioinspired peptide amphiphiles. The design principle was inspired by the oligomerization of the human immunodeficiency virus type-1 (HIV-1) Rev prot...
متن کاملC-terminal fragments of APP: Its neurotoxic mechanisms and involvement in gene transcription
Several lines of evidence suggest that some neurotoxicity in AD is due to proteolytic fragments of APP. In this study, we compared the potency of neurotoxicity induced by CT with that of A-beta neurotoxicity and our results showed that various CT peptide fragments (CTFs; CTF99, AICD, CTF31) caused neurotoxicity in cultured cells and primary cortical neurons, induced strong non-selective inward ...
متن کاملC-terminal fragments of APP: Its neurotoxic mechanisms and involvement in gene transcription
Several lines of evidence suggest that some neurotoxicity in AD is due to proteolytic fragments of APP. In this study, we compared the potency of neurotoxicity induced by CT with that of A-beta neurotoxicity and our results showed that various CT peptide fragments (CTFs; CTF99, AICD, CTF31) caused neurotoxicity in cultured cells and primary cortical neurons, induced strong non-selective inward ...
متن کاملApplication of FITC for detecting the binding of antiangiogenic peptide to HUVECs
Angiogenesis is the generation of new blood vessels from the existing vasculature. The angiogenic programme requires the degradation of the basement membrane, endothelial cell migration and invasion of the extracellular matrix, with endothelial cell proliferation and capillary lumen formation before maturation and stabilization of the new vasculature. Angiogenesis is dependent on a delicate equ...
متن کامل