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Evaluation Methods for Conditioned Hair
Published in E. Desmond Goddard, James V. Gruber, Principles of Polymer Science and Technology in Cosmetics and Personal Care, 1999
E. Desmond Goddard, James V. Gruber
the chemical composition of low-sulfur filament keratins with sequences of helical and nonhelical domains of various lengths. They replaced the term “microfibrils” with the term “intermediate filaments” (IF), which has its origin in cellular biology describing structural protein fibrils in the cytoskeleton of cells and is also being used to describe the nature of keratin filaments in the keratocytes of the epidermal stratum corneum. The matrix between the keratin intermediate filaments in the cortex consists of various families of keratin-associated proteins (KAP), which are mostly rich in cystine but also include various proteins rich in glycine and tyrosine. Zahn has been particularly active in promoting the general acceptance of this new nomenclature, and it has been incorporated by Robbins into the third edition of his book Chemical and Physical Behavior of Human Hair (8). Medulla
Nanoindentation of Hair Fiber: A Tough Hierarchical Layered Architecture
Published in Arjun Dey, Anoop Kumar Mukhopadhyay, Nanoindentation of Natural Materials, 2018
Aniruddha Samanta, Manjima Bhattacharya, Anoop Kumar Mukhopadhyay, Shekhar Nath, Arjun Dey
Another important recent effort [14] has attempted to classify the most vital component of hair, for example, the keratin-associated proteins (KAPs), in terms of their respective sulphur contents. It has been accordingly noted [14] that the KAPs can be classified into three groups; high sulfur (HS) KAPs, ultra high sulfur (UHS) KAPs, and high glycine-tyrosine (HGT) KAPs.
Evaluating the antioxidant effects of human hair protein extracts
Published in Journal of Biomaterials Science, Polymer Edition, 2018
Hui Ying Lai, Shuai Wang, Vaishali Singh, Luong T. H. Nguyen, Kee Woei Ng
Keratin is a class of intermediate filament structural proteins that can be found in the epidermis and epidermal appendages of vertebrates such as wool, nails, feathers, hooves, and hair. Together with keratin associated proteins (KAPs), they confer unique mechanical properties found in the epidermal appendages. As biomaterials, these proteins exhibit tremendous potential as regenerative substrates due to their inherent biocompatibility, biodegradability and bioactivity [1–4]. Keratins and KAPs derived from human hair offer several advantages over its animal counterparts due to its potentially lower immunogenicity and the possibility to personalize autologous material platforms depending on the patient’s needs. Abundant and readily available supplies of human hair make this an economical source of human-derived bioactive biomaterials. To this end, keratin-based coatings, films, hydrogels, sponges, and fibers have been explored in various tissue engineering and regenerative medicine applications [5–10].