Dr hab.
Alina Sionkowska (PhD, DSc)
Faculty of Chemistry,
NCU Toruń
as@chem.uni.torun.pl
Photochemical processes are important in vision and
photosynthesis, which are the most representative biological processes.
However, the gradual changes in the properties of materials which occur on
exposure to sun light are well known.
The effects of
ultraviolet radiation are both advantageous and deleterious to living
organisms. Ultraviolet light has been used since 1877 to sterilise foods, to maintain
sterile conditions during surgery, for preventing rickets, for killing pests
and insects and for many other purposes. Ultraviolet light absorption is
responsible for skin tanning and has been implicated in a causative way in many
kinds of skin cancer.
Collagen is
the most abundant protein in animals where it provides the principal structural
and mechanical support [1,2]. There are 20 genetically distinct collagens in
the collagen family, the major fibril forming collagens: type I ( skin, tendon
and bone), type II (cartilage) and type III (skin and vasculature) are found as
part of fibrillar structures that form an essential part of tissue architecture
and integrity. Collagen is readily available, non-toxic and the fibril
architecture that is inherent in natural tissues means that it provides an
excellent basis for biomaterials such as arterial prostheses and artificial
skin [3,4]. The degradation of biomaterials is an important factor in the
suitability of using collagen in prostheses and many attempts have been made to
alter the degradation properties of collagen.
Environmental
factors such as UV irradiation that are able to modulate the structure and
chemistry of collagen in vivo and in vitro therefore have a twofold importance.
Although there have been a number of previous attempts to investigate
the effects of UV irradiation on collagen, the results have been far from
conclusive with the emphasis often being on only one aspect of UV photodamage
such as the biomechanical or biochemical effects. There is poor agreement
as to whether the main effect of UV
irradiation on collagen is.
Crosslink
formation between collagen molecules, this is characterised by the decrease
observed in collagen solubility after UV irradiation. Some preliminary evidence
from my studies indicates the possibility of the formation of both inter and
intramolecular crosslinking. Bond
scission has been demonstrated by a number of research groups, this is
characterised by a characteristic decrease in viscosity and the changes of
absorbances point to the loss of water bonded to collagen, degradation of the
peptide chains with scission of the amide bonds and abstraction of the side
groups [5-11].
The photodamage of specific residues that allows the development of chromophores may
be related to the above properties however the changes have been mainly
characterised by spectrophotometry without detailed amino acid analysis. The formation of dityrosine has been reported by some research groups [12,13].
From the
foregoing it can be seen that an understanding of photomodification is
essential to the development of strategies able to alter the emphasis of
bond scission, crosslinkage and photodamage.
References
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