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The novel HLA-A*68:100 allele differs from HLA-A*68:01:02:01 by one nucleotide substitution in exon 3 at position 371.

HLA-B*15:271 differs from HLA-B*15:25:01 by 1 nucleotide substitution at codon 197 in exon 4.

HLA-B*27:103 has one nucleotide change from HLA-B*27:04:01 at position 121C T.

Collagen solutions in the presence of 0.1–2.0M acetic acid (AA) were investigated to understand the interaction between collagen molecules and an acidic solvent. Fluorescence measurements of pyrene showed that the critical aggregation concentration (CAC) of collagen increased from 0.518 to 1.581 mg/mL for AA concentrations ranging from 0.1 to 2.0M, indicating that the aggregated state of collagen molecules was associated with AA concentration. The size of the collagen aggregates, determined by dynamic light scattering, demonstrated that their disaggregation was enhanced with increasing electrostatic repulsion between the collagen chains. The variations in the intrinsic viscosity and Huggins coefficient depended on the molecular interaction among the collagen molecules. Furthermore, the increased AA concentration has a different influence on the rigidity of collagen molecules above and below the CAC. This observation was manifested by the changes in the morphology of collagen molecules observed by atomic force microscopy. © 2017 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2017, 134, 45255.

The surface activity of pepsin-solubilized type I collagen acylated by lauroyl chloride and succinic anhydride was investigated in this article. Compared with native collagen, acylated collagen exhibited better surface activity such as oil absorption capacity, emulsion activity and stability, foam expansion, and foam stability but presented lower water absorption capacity. Acylated collagen also had higher emulsion activity and stability than Tween 80, whereas Tween 80 displayed higher foam expansion and stability than acylated collagen. After acylation, the surface tension of collagen decreased with the storage time increased, the hydrophobicity and the wetting power increased with the increase of the concentration. Meanwhile, the emulsion activity and stability of acylated collagen decreased with the increase of NaCl concentration ranging from 20 to 100 mmol/L. Under neutral pH value, acylated collagen reached higher emulsion activity and stability at acylated collagen concentration of 0.4 mg/mL and lower temperature (

Collagen/HPMC blends with different HPMC content (HC) were investigated by dynamic responses, creep recovery, thixotropy, and morphological observation. Storage modulus, loss modulus, complex viscosity, and activation energy decreased with the increased HC, while the flow behavior index increased with the increased HC and the dynamic denaturation temperature reached the maximum as HC increased to 50%, indicating that the flowability and thermal stability of collagen solution were improved by the addition of HPMC. However, the blends with higher HC tended to have a relatively lower recovery capacity, and the hysteresis loop areas of the blends were lower than that of collagen (especially when HC > 50%). Additionally, the morphology of collagen/HPMC was examined by both of atomic force microscopy and scanning electron microscopy. By combining with these results, it seemed that the rheological and structural properties of collagen/HPMC were related to the hydrogen-bond interaction and compatibility between collagen and HPMC molecules. © 2013 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2014, 131, 40042.