amphipathic


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amphipathic

(ˌæmfɪˈpæθɪk) or

amphipath

adj
(Biochemistry) chem biochem of or relating to a molecule that possesses both hydrophobic and hydrophilic elements, such as are found in detergents, or phospholipids of biological membranes
References in periodicals archive ?
This nanocarrier is a neutral, amphipathic and biodegradable nano-material synthesized previously by our group (Sarbolouki et al.
Adsorption of peripheral proteins to a phospholipid surface often depends on defects in packing of lipid molecules, which enable insertion of amphipathic helices.
Still, these peptides have small size and diversity in secondary structure and composition but the following features shared among them including positive charge, high content of hydrophobic residues, amphipathic fold, ease of synthesis and modification and tumor penetrating ability [1719].
As amphipathic material, the hydrophilic portion at the surface has likely a preference to the polar acrylonitrile segment of the blend whilst the hydrophobic part will be directed in a preferential way to the styrene-butadiene segment.
Among AMPs, cecropins (Cec) are small (~4 kDa) peptides containing 35 to 39 amino acids, which are amphipathic, as a high proportion of basic amino acids are present at the N-terminus conferring a net positive charge and the hydrophobic amino acids are rich at the C-terminus (Sipos et al.
Siva-1 consists of several distinct domains: an N-terminal region, a putative amphipathic helical (SAH) region, a death domain homology region (DDHR), and a C-terminal cysteine-rich region that includes a B-BOX domain and a zinc-finger-like domain (2,3).
7) It is this amphipathic behavior that can be used to disperse the oil slick.
Amphipathic lipid metabolites and their relation to arrhythmogenesis in the ischemic heart.
Polymersomes are giant vesicles that are made from amphipathic block copolymers.
showed that this mutation occurs in a region of the perforin protein that exhibits amphipathic conformation in order to interact with and traverse the membrane lipid bilayer, and exhibits the highest degree of homology to the putative lipid-binding domain of the complement components.
This process involves a concerted conformational change whereby two regions of each CDC monomer, which are initially in an a-helical conformation, refold into an extended conformation and insert into the bilayer as two amphipathic [beta]-hairpins (TMH).
Among many strategies, studies on natural and artificial amphipathic peptides acting on membranes of microorganisms have yielded promising results.