Self‐assembling amphiphilic peptides

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Self-assembling amphiphilic peptides†

The self-assembly of several classes of amphiphilic peptides is reviewed, and selected applications are discussed. We discuss recent work on the self-assembly of lipopeptides, surfactant-like peptides and amyloid peptides derived from the amyloid-β peptide. The influence of environmental variables such as pH and temperature on aggregate nanostructure is discussed. Enzyme-induced remodelling due...

متن کامل

Structures, function and applications of amphiphilic peptides

Major recent ad ances: Amphiphilic peptides, in other words, peptides that contain hydrophobic and hydrophilic regions along their lengths, have been molecularly designed and exploited in various ways. Most notable advancements in the past few years are their proposed use for scaffolds for nanometer structures such as molecular wires and mineralization of hydroxyapatite crystals in a particular...

متن کامل

PEG-stabilized lipid disks as carriers for amphiphilic antimicrobial peptides.

Antimicrobial peptides hold potential as a possible alternative, or complement, to conventional antibiotics but new, safe and efficient means are needed for formulation and administration of the peptides. In this study we have investigated the utility of a novel type of lipid particles, the polyethylene glycol-stabilized lipid disks, as carriers for the model peptide melittin. The structural in...

متن کامل

Membrane disruption ability of facially amphiphilic helical peptides.

A helical 14-residue peptide containing four polar, but uncharged, benzo-21-crown-7 side-chains aligned along one face induces significantly more vesicle leakage than analogous 21-mer or 7-mer peptides.

متن کامل

Elasticity of Lipid Bilayer Interacting with Amphiphilic Helical Peptides

Amphiphilic helical peptides exhibit an insertion transition when they interact with lipid bilayers. At low concentrations, the peptides adsorb at the hydrophilic-hydrophobic interface with the helical axes parallel to the bilayer surface. However, if the peptide concentration is above a critical value, a macroscopic fraction of the peptide molecules insert perpendicularly into the bilayer. The...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Journal of Peptide Science

سال: 2014

ISSN: 1075-2617,1099-1387

DOI: 10.1002/psc.2633