Moreover, the amphipathic
helix was required for activity .
Hama et al., "Effects of increasing hydrophobicity on the physical-chemical and biological properties of a class A amphipathic
helical peptide," Journal of Lipid Research, vol.
Merisko-Liversidge, "Direct suppression of phagocytosis by amphipathic
polymeric surfactants," Pharmaceutical Research, vol.
Yewdell, "The influenza A virus PB1-F2 protein targets the inner mitochondrial membrane via a predicted basic amphipathic
helix that disrupts mitochondrial function," Journal of Virology, vol.
It is known as a hemolytic peptide which have 26 amino acid and amphipathic
a-helices (Raghuraman and Chattopadyay 2007).
The lipid-binding region encompasses residues 240 -270 in the carboxyl-terminus, which form an amphipathic
In general, gram-negative bacteria have an effective outer membrane that restricts the penetration of amphipathic
compounds and has a mechanism to extrude toxins across .
The autotransporter proteins of Gram-negative bacteria exhibit an N-terminal signal sequence, required for secretion across the inner membrane, and a C-terminal domain that forms an amphipathic
[beta]-barrel pore that allows passage of the functional domain across the outer membrane.
Cholesterol is a polycyclic amphipathic
molecule derived from a sterane backbone (Figure 1).
Cai, "Prediction of membrane protein types by incorporating amphipathic
effects," Journal of Chemical Information and Modeling, vol.
Structural modeling of Tp0326 predicted five polypeptide transport-associated (POTRA) domains in the N-terminus and 18-stranded amphipathic
[beta]-barrel in the C-terminus, which are responsible for the native protein's amphiphilicity  (Figure 1).
[alpha]-Synuclein consists of 140 amino acid residues  organized in three structural regions: an amphipathic
amino-terminal domain from 1 to 60 amino acid residues, responsible for the binding of [alpha]-synuclein to lipid vesicles [25, 26]; the NAC (non-amyloid-[beta] component) region from 61 to 95 amino acid residues, also found in amyloid plaques of patients suffering from Alzheimer's disease  and responsible for [alpha]-synuclein aggregation and [beta] sheets arrangement ; and the carboxy-terminal domain from 96 to 140 amino acid residues, which is the main target for the protein phosphorylation [29, 30] (Figure 1(a)).