Potential of human γD‐crystallin for hair damage repair: insights into the mechanical properties and biocompatibility. (21st June 2013)
- Record Type:
- Journal Article
- Title:
- Potential of human γD‐crystallin for hair damage repair: insights into the mechanical properties and biocompatibility. (21st June 2013)
- Main Title:
- Potential of human γD‐crystallin for hair damage repair: insights into the mechanical properties and biocompatibility
- Authors:
- Ribeiro, A.
Matamá, T.
Cruz, C. F.
Gomes, A. C.
Cavaco‐Paulo, A. M. - Abstract:
- <abstract abstract-type="main" id="ics12065-abs-0001"> <title>Synopsis</title> <sec id="ics12065-sec-0001" sec-type="section"> <title>Objectives</title> <p>The objective of this work was to develop a new strategy to physically 'repair' chemically damaged hair. Hence the human eye γD‐crystallin, a protein from the superfamily characterized structurally by the Greek key motif, was studied. The human γD‐crystallin was chosen based on the ability of proteins belonging to this superfamily to be involved in the coating of specific structures. Two crystallins were used on the study, the wild type (Protein Data Bank ID: 1HK0) and the mutant protein. The mutant form was intended to induce a strong and quick protein polymerization as well to have new possible points of anchorage to hair.</p> </sec> <sec id="ics12065-sec-0002" sec-type="section"> <title>Methods</title> <p>The ability of both crystallins to bind to damaged hair and even penetrate into its cortex was checked by fluorescence microscopy, confocal microscopy and scanning electron microscopy. Furthermore the reinforcement of hair mechanical resistance, the potential cytotoxic/inflammatory effect of crystallins were studied in order to have a fully comprehension about the protein based formulation.</p> </sec> <sec id="ics12065-sec-0003" sec-type="section"> <title>Results</title> <p>Although the chemical over‐bleaching treatment induced a decrease of 20% on the resistance of the hair, the crystallins which bind and penetrate<abstract abstract-type="main" id="ics12065-abs-0001"> <title>Synopsis</title> <sec id="ics12065-sec-0001" sec-type="section"> <title>Objectives</title> <p>The objective of this work was to develop a new strategy to physically 'repair' chemically damaged hair. Hence the human eye γD‐crystallin, a protein from the superfamily characterized structurally by the Greek key motif, was studied. The human γD‐crystallin was chosen based on the ability of proteins belonging to this superfamily to be involved in the coating of specific structures. Two crystallins were used on the study, the wild type (Protein Data Bank ID: 1HK0) and the mutant protein. The mutant form was intended to induce a strong and quick protein polymerization as well to have new possible points of anchorage to hair.</p> </sec> <sec id="ics12065-sec-0002" sec-type="section"> <title>Methods</title> <p>The ability of both crystallins to bind to damaged hair and even penetrate into its cortex was checked by fluorescence microscopy, confocal microscopy and scanning electron microscopy. Furthermore the reinforcement of hair mechanical resistance, the potential cytotoxic/inflammatory effect of crystallins were studied in order to have a fully comprehension about the protein based formulation.</p> </sec> <sec id="ics12065-sec-0003" sec-type="section"> <title>Results</title> <p>Although the chemical over‐bleaching treatment induced a decrease of 20% on the resistance of the hair, the crystallins which bind and penetrate the hair fibre were able to recover and even to improve its mechanical properties when compared to the virgin hair. Moreover none of the crystallins displayed a toxic effect in fibroblasts for all the range of tested concentrations upon 72 h of exposure. The active aggregation process of mutant crystallin induced an inflammatory response in fibroblasts in the first 24 h of contact, measured by the amount of released pro‐inflammatory cytokine IL‐6 to the medium. In contrast contact with wild type crystallin did not lead to significant inflammation.</p> </sec> <sec id="ics12065-sec-0004" sec-type="section"> <title>Conclusion</title> <p>Outcome from protein formulation characterization supports the hypothesis that the γD‐crystallin it is able to recover and improve the mechanical properties of chemical damaged hair. Therefore it can be considered as a very promising strengthening agent for the development of new restorative hair care products.</p> </sec> </abstract> … (more)
- Is Part Of:
- International journal of cosmetic science. Volume 35:Number 5(2013:Oct.)
- Journal:
- International journal of cosmetic science
- Issue:
- Volume 35:Number 5(2013:Oct.)
- Issue Display:
- Volume 35, Issue 5 (2013)
- Year:
- 2013
- Volume:
- 35
- Issue:
- 5
- Issue Sort Value:
- 2013-0035-0005-0000
- Page Start:
- 458
- Page End:
- 466
- Publication Date:
- 2013-06-21
- Subjects:
- Cosmetics -- Periodicals
668.5505 - Journal URLs:
- http://www.blackwell-synergy.com/member/institutions/issuelist.asp?journal=ics ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1468-2494 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/ics.12065 ↗
- Languages:
- English
- ISSNs:
- 0142-5463
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4542.178400
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3005.xml