Unusual fragmentation pathways in collagen glycopeptides.
Unusual fragmentation pathways in collagen glycopeptides.
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DOI：
10.1007/s13361-013-0624-y
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发表时间：
2013-07
影响因子：
3.2
通讯作者：
Tomer, Kenneth B.
中科院分区：
文献类型：
--
作者：
Perdivara, Irina;Perera, Lalith;Sricholpech, Marnisa;Terajima, Masahiko;Pleshko, Nancy;Yamauchi, Mitsuo;Tomer, Kenneth B.
关键词：
胶原蛋白是体内最丰富的糖蛋白。该蛋白家族的一个特征是氨基酸序列由三个氨基酸（X-Y-Gly）n的重复组成。在这个基序中，Y残基通常是4-羟脯氨酸（HyP）或5-羟赖氨酸（HyK）。胶原中的糖基化发生在HyK中的5-OH基团上，以两种糖苷的形式，半乳糖基羟基赖氨酸（Gal-HyK）和葡萄糖基半乳糖基羟基赖氨酸（GlcGal-HyK）。在碰撞诱导解离（CID）中，与典型的N-和o -键糖肽相比，胶原色氨酸糖肽表现出意想不到的气相解离行为，即除了糖苷键断裂外，还观察到广泛的酰胺键断裂。Gal-或GlcGal-聚糖修饰大部分保留在片段离子上。这些特征使胶原糖肽的氨基酸序列和糖基化位点的位置的明确测定。这种解离模式对所有分析的胶原糖肽是一致的，无论其长度或氨基酸组成，胶原类型或组织。两种断裂途径-酰胺键和糖苷键裂解-在胶原色氨酸中是高度竞争的。相对于碱性位点（即Arg， Lys， HyK和n端）的电离质子数是断裂的主要驱动力。本文采用量子力学计算方法，对胶原糖肽气相解离过程中增强酰胺键不稳定性和羟赖氨酸苷稳定性的因素进行了研究。
Collagens are the most abundant glycoproteins in the body. One characteristic of this protein family is that the amino acid sequence consists of repeats of three amino acids –(X—Y—Gly)n. Within this motif, the Y residue is often 4-hydroxyproline (HyP) or 5-hydroxylysine (HyK). Glycosylation in collagen occurs at the 5-OH group in HyK in the form of two glycosides, galactosylhydroxylysine (Gal-HyK) and glucosyl galactosylhydroxylysine (GlcGal-HyK). In collision induced dissociation (CID), collagen tryptic glycopeptides exhibit unexpected gas-phase dissociation behavior compared to typical N- and O-linked glycopeptides, i.e. in addition to glycosidic bond cleavages, extensive cleavages of the amide bonds are observed. The Gal- or GlcGal- glycan modifications are largely retained on the fragment ions. These features enable unambiguous determination of the amino acid sequence of collagen glycopeptides and the location of the glycosylation site. This dissociation pattern was consistent for all analyzed collagen glycopeptides, regardless of their length or amino acid composition, collagen type or tissue. The two fragmentation pathways – amide bond and glycosidic bond cleavage – are highly competitive in collagen tryptic glycopeptides. The number of ionizing protons relative to the number of basic sites (i.e. Arg, Lys, HyK and N-terminus) is a major driving force of the fragmentation. We present here our experimental results and employ quantum mechanics calculations, to understand the factors enhancing the labile character of the amide bonds and the stability of hydroxylysine glycosides in gas phase dissociation of collagen glycopeptides.
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影响因子：
4.4
作者：
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通讯作者：
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影响因子：
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作者：
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DOI：
10.1016/1044-0305(95)00682-6
发表时间：
1996-04-01
影响因子：
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作者：
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通讯作者：
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影响因子：
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作者：
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影响因子：
--
作者：
Liefhebber, Jolanda M. P.;Punt, Simone;Spaan, Willy J. M.;van Leeuwen, Hans C.
通讯作者：
van Leeuwen, Hans C.