Investigation of the relationship between the rodlet formation and Cys3-Cys4 loop of the HGFI hydrophobin.

摘要: We used protein fusion technology to transplant the Cys3-Cys4 loop of HGFI (a class I hydrophobin from Grifola frondosa) into a nonamyloidogenic HFBI II Trichoderma reesei) and replace corresponding amino acids between Cys3 Cys4 in this identify whether renders it amyloidogenic. Water contact angle (WCA) X-ray photoelectron spectroscopy (XPS) measurements demonstrated that mutant HFBI-AR could form amphipathic membranes by self-assembling at hydrophilic mica hydrophobic polystyrene surfaces. This property enabled alter surface wettabilities as well change elemental composition siliconized glass. Atomic force microscopy (AFM) indicated that, unlike hydrophobins, no amyloid-like rodlets were observed on coated surface. Moreover, region not catalyze drive intermolecular association formation cross-β rodlet structure resist depolymerization organic solvents when self-assembled water-air interfaces. These results demonstrate is major determinant initiates or account for unique properties proteins.