Sg. Summerfield et al., INTRA-IONIC INTERACTIONS IN ELECTROSPRAYED PEPTIDE IONS, International journal of mass spectrometry and ion processes, 162(1-3), 1997, pp. 149-161
Citations number
20
Categorie Soggetti
Spectroscopy,"Physics, Atomic, Molecular & Chemical
Recent studies have demonstrated that interactions between cysteic aci
d and arginine residues have a marked effect on the low energy decompo
sitions of protonated peptides in the gas phase. This work extends the
se findings to show that analogous interactions operate in the presenc
e of other acidic amino acid residues, although the effects are less p
ronounced. Thus, the presence of aspartic or glutamic acid residues (X
) in the sequence, RLXIFSXFR, attenuates the proton-sequestering prope
rties of the arginine residues in the [M+2H](2+) ion, thereby promotin
g charge-proximal fragmentation of the peptide backbone. Significant d
ifferences in fragmentation behavior are observed for the doubly proto
nated peptide incorporating two aspartic acid residues, in comparison
with the glutamic acid-containing analogue. Low energy collisional act
ivation of [M+2H](2+) ions of RLDIFSDFR, but not RLEIFSEFR, yields sig
nificant d-type ions associated with cleavage at the acidic residues.
The proposed mechanism invokes arginine/aspartic acid side-chain inter
action and is blocked by the additional methylene group in the glutami
c acid side-chain. b-Type fragmentation is promoted C-terminal to the
aspartic acid residues; this is attributed to nucleophilic attack of t
he side-chain carboxyl group on the carbonyl carbon of the adjacent pe
ptide bond and is promoted by an interaction between the acidic side c
hain and the guanidino group of the N-terminal arginine residue, This
effect is not observed for the glutamic acid-containing analogue. Mole
cular mechanics calculations indicate lowest energy conformations cons
istent with the mass spectrometric data; specifically, the additional
methylene group in the glutamic acid side-chain markedly increases the
distance between the carboxyl group and the adjacent peptide bond. (C
) 1997 Elsevier Science B.V.