TY - JOUR
T1 - Polymeric peptide pigments with sequence-encoded properties
AU - Lampel, Ayala
AU - McPhee, Scott A.
AU - Park, Hang-Ah
AU - Scott, Gary G.
AU - Humagain, Sunita
AU - Hekstra, Doeke R.
AU - Yoo, Barney
AU - Frederix, Pim W. J. M.
AU - Li, Tai-De
AU - Abzalimov, Rinat R.
AU - Greenbaum, Steven G.
AU - Tuttle, Tell
AU - Hu, Chunhua
AU - Bettinger, Christopher J.
AU - Ulijn, Rein V.
N1 - This is the author's version of the work. It is posted here by permission of the AAAS for personal use, not for redistribution. The definitive version was published in
Science on 09 June 2017 in volume 356, DOI: 10.1126/science.aal5005.
PY - 2017/6/9
Y1 - 2017/6/9
N2 - Melanins are a family of heterogeneous polymeric pigments that provide ultraviolet (UV) light protection, structural support, coloration, and free radical scavenging. Formed by oxidative oligomerization of catecholic small molecules, the physical properties of melanins are influenced by covalent and noncovalent disorder. We report the use of tyrosine-containing tripeptides as tunable precursors for polymeric pigments. In these structures, phenols are presented in a (supra-)molecular context dictated by the positions of the amino acids in the peptide sequence. Oxidative polymerization can be tuned in a sequence-dependent manner, resulting in peptide sequence–encoded properties such as UV absorbance, morphology, coloration, and electrochemical properties over a considerable range. Short peptides have low barriers to application and can be easily scaled, suggesting near-term applications in cosmetics and biomedicine.
AB - Melanins are a family of heterogeneous polymeric pigments that provide ultraviolet (UV) light protection, structural support, coloration, and free radical scavenging. Formed by oxidative oligomerization of catecholic small molecules, the physical properties of melanins are influenced by covalent and noncovalent disorder. We report the use of tyrosine-containing tripeptides as tunable precursors for polymeric pigments. In these structures, phenols are presented in a (supra-)molecular context dictated by the positions of the amino acids in the peptide sequence. Oxidative polymerization can be tuned in a sequence-dependent manner, resulting in peptide sequence–encoded properties such as UV absorbance, morphology, coloration, and electrochemical properties over a considerable range. Short peptides have low barriers to application and can be easily scaled, suggesting near-term applications in cosmetics and biomedicine.
KW - ultraviolet light protection
KW - UV
KW - melanins
KW - polymeric peptide pigments
UR - http://science.sciencemag.org/
U2 - 10.1126/science.aal5005
DO - 10.1126/science.aal5005
M3 - Article
SN - 1095-9203
VL - 356
SP - 1064
EP - 1068
JO - Science
JF - Science
IS - 6342
ER -
