amphipathic


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am·phi·path·ic

(am'fē-path'ik),
Denoting a molecule, such as comprises detergents or wetting agents, which contains groups with characteristically different properties, for example, both hydrophilic and hydrophobic properties.
Synonym(s): amphiphilic, amphiphobic
[amphi- + G. pathos, feeling]

amphipathic

[-path′ik]
Etymology: Gk, amphi both + pathos suffering
pertaining to a molecule having two sides with characteristically different properties, such as a detergent, which has both a polar (hydrophilic) end and a nonpolar (hydrophobic) end but is long enough so that each end demonstrates its own solubility characteristics.

amphipathic

Of a chemical structure having both hydrophobic and hydrophilic surfaces as in the case of the phospholipid molecules of the cell membrane. Some proteins have amphipathic regions.

amphipathic

a molecule containing both HYDROPHILIC and HYDROPHOBIC components, as in a phospholipid molecule. See FLUID-MOSAIC MODEL.

amphipathic

molecules containing both polar and non-polar regions in their structure.
References in periodicals archive ?
Amphipathic hyperbranched polymeric thioxanthone photoinitiators (AHPTXs): Synthesis, characterization and photoinitiated polymerization.
NS5A has an amphipathic alpha-helix at its amino terminus with which it is anchored to the ER membrane.
Strands 2 and 3 of the [beta]-sheet run the length of the protein, forming a positively charged amphipathic hairpin loop with a [beta]-turn (residues 32 50).
The heterotrimeric G protein is responsible for signal transduction with a major receptors class G-protein-coupled receptors (GPCR), an integral membrane proteins that have seven amphipathic helices (7TM) (8), and participates in cardiovascular reflexes.
Shampoos comprise amphipathic molecules called surfactants that self assemble into nano-scale micelles.
The influenza A virus PB1-F2 protein targets the inner mitochondrial membrane via a predicted basic amphipathic helix that disrupts mitochondrial function.
Researchers have produced an 18-amino-acid peptide that mimics the structure of a portion of the amphipathic, helical peptide that forms apo [A.
The aqueous phase contains amphipathic and polar material and the chloroform phase the lipid compounds (Home and McIntosh 2000).
These synthetic peptides link the high-affinity binding domain of Apo-E to an amphipathic peptide that has a high affinity for lipid rich lipoproteins.
The technology offers potential benefits for the delivery of lipophilic and amphipathic molecules and proteins for topical applications in a cost-effective system with proven flexibility and cosmetic elegance.