Bulletin USAMV-CN, 63 - 64/2007
AMINO ACIDS SEQUENCE ANALYSIS ON COLLAGEN
Sorana D. Bolboaca 1, Jantschi L 2
1“Iuliu Hatieganu” University of Medicine and Pharmacy Cluj-Napoca, 6 Louis Pasteur, 400349 Cluj-
Napoca, Romania, [email protected]
2Technical University of Cluj-Napoca, 103-105 Muncii Bvd., 400641 Cluj-Napoca, Romania.
[email protected]
Key words: Amino Acids; Collagen Type I; Properties; Multivariate Analysis
Abstract. Staring from available information about amino acids properties and sequences on collagen
type I chains, the aims of the study were to identify the principal property component and to analyze the
similarities within and between collagens on five species. The principal component analysis applied on twenty-
four amino acids properties revealed that the hydrophobic or hydrophilic character measured by Wealling et al. is
more stable comparing with the other investigated properties. Similarity analysis identified similar and dissimilar
within and between studied species from the viewpoint of amino acids sequences on collagen type I alpha 1 and
2 chains.
INTRODUCTION
Collagen, the main protein of connective tissues, is a fibrous protein, inextensible,
which can be found at the level of connective tissues from heart, vessels, skin, cornea,
cartilage, ligaments, tendons, bone, and teeth. Today are known twenty-eight types of
collagens (Veit et al., 2006).
The structure of collagen type I, distributed at the level of all tissues in organism, is
known from a long time (Kadler et al., 1996). The COL1A1 and COL1A2 genes which
coding the collagens chains have also been identified and characterized: Homo Sapiens (Chu
et al., 1985; Runyan et al., 2003), Rattus Norvegicus (Kwitek et al., 2004; Malfait et al.,
2006). Due to its implications in osteogenesis imperfecta (Lee et al., 2006), osteoporosis
(Ralston et al., 2006), Ehlers-Danlos syndrome (Pollitt et al, 2006), Caffey disease (Gensure
et al., 2005), to possible implication in other diseases (e.g. intracranial aneurysms -
Yoneyama et al., 2004), as indicator of bone metastasis - Fukumitsu et al., 2003) the collagen
type I is studied by many researchers.
Based on information about amino acids properties and sequences on collagen type I
chains, the aims of the study were to identify the principal property component and to analyze
the similarities within and between collagens on five species.
MATERIAL AND METHOD
Amino Acids Properties
The sample of twenty essential amino acids with twenty-four associated properties has
been investigated. The studied properties were: hydrophobic or hydrophilic character
measured on different scales (p1 - Black et al., 1991; p2 - Kyte and Doolittle, 1982; p3 -
Wimley and White, 1996; p4 - Hessa et al., 2005; p5 - Sereda et al., 1994; p6 - Hoop and
Woods, 1981; p7 - Cornette et al., 1987; p8 - Eisenberg et al., 1984; p9 - Rose et al., 1985; p10
- Janin, 1979; p11 - Engelman et al., 1986; p12 - Sweet and Eisenberg, 1983; p14 - Bull and
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