Temperature dependence of photochemical fluorescence fading in Skh-1 hairless mouse collagen.
BACKGROUND
Type I mammalian collagens have several photolabile fluorescent moieties that absorb UV rays capable of reaching the dermis. We studied the temperature dependence of fluorescence fading as a marker of photochemical damage.


METHODS
Collagen solutions were exposed to radiation from 0 to 240 min from either a UVG-11 hand lamp, total dose=1.173 x 10(3) J/m(2); a UVL-21 hand lamp total dose=2.030 x 10(3) J/m(2); or the fluorometer, at 325+/-5 nm, total dose=0.156 x 10(3) J/m(2). We recorded intensities at excitation/emission wavelengths 270/300, 270/330, 270/360, 270/400, 325/400, and 370/450 nm at T=9.0-59.3 degrees C.


RESULTS
Results indicated simultaneous forward and reverse reactions. However, the 270/360 nm fluorophore could be analyzed as a second-order reaction. The Arrhenius curve showed two straight lines intersecting near the denaturation temperature, with helix activation energy E(a) approximately 0 and coil E(a)=7.6+/-0.6 kcal/mol (31.7+/-2.5 kJ/mol).


CONCLUSIONS
Collagen-bound fluorophores are not just passive markers of oxidative stress and age-related damage. Their photolability to wavelengths reaching the dermis may result in pathological conditions, particularly at elevated body temperatures.
Department of Microbiology/Biochemistry/Immunology, Morehouse School of Medicine, Atlanta, GA 30310-1495, USA. jmenter@msm.edu
Julian M
JM
Menter
Eugenia G
EG
Chu
Nicolle V
NV
Martin
D000818:Animals; D024042:Collagen Type I / Q000737:chemistry*; D005453:Fluorescence; D051379:Mice; D008812:Mice, Hairless; D010777:Photochemistry; D013696:Temperature
D024042:Collagen Type I