Solution and solid-state circular dichroism analyses of a human salivary proline-rich glycoprotein repeating domain and its subfragments

González, Mendoza; Loomis, Pamela M.; Loomis, Ronald E.

doi:10.1016/0141-8130(93)90018-h

Cited by 2 publications

(3 citation statements)

References 27 publications

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“…This tendency to increase the PPII content at acid pH is in accordance with previously reported data. 19,22,23 This effect may reflect the fact that solvation of proline carbonyl groups is optimal in a PPII conformation, and this solvation requirement is stronger at acidic pH, when carbonyl groups can start to become protonated. 19,[22][23][24][25] When X is glutamic acid (Figure 7b), the magnitude of the λ min and λ max values decrease as the pH is lowered to pH 3.…”

Section: Discussionmentioning

confidence: 99%

“…19,22,23 This effect may reflect the fact that solvation of proline carbonyl groups is optimal in a PPII conformation, and this solvation requirement is stronger at acidic pH, when carbonyl groups can start to become protonated. 19,[22][23][24][25] When X is glutamic acid (Figure 7b), the magnitude of the λ min and λ max values decrease as the pH is lowered to pH 3. This anomalous behavior of H-(Val-Glu-Leu-Pro-Pro-Pro) 8 -OH is probably due to protonation of the carboxyl groups in the side-chain of glutamic acid residues at pH 3, and side chain-side chain and/or side chain-backbone interactions, via hydrogen bonding, may then become more important and affect the conformational equilibrium.…”

Section: Discussionmentioning

confidence: 99%

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Convergent Synthesis of Repeating Peptides (Val-X-Leu-Pro-Pro-Pro)₈Adopting a Polyproline II Conformation

et al. 1996

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The N-terminal domain of maize gamma-zein has a repetitive structure (Val-His-Leu-Pro-Pro-Pro)(8) that has recently been shown to adopt an amphipathic polyproline II type conformation in aqueous solution. We report here the synthesis and conformational analysis of three model peptides (Val-X-Leu-Pro-Pro-Pro)(8) (X = Ala (1), Glu (2), Lys (3)). The three compounds have been synthesized in a very efficient way using a convergent solid-phase strategy. Circular dichroism shows unequivocally that the three model peptides adopt polyproline II (PPII) type conformations under a variety of experimental conditions and that neither the presence of histidine nor amphipathicity of the peptide is an absolute requirement for adopting the native conformation. These results open the door for the de novo design of compounds with PPII conformations and must be taken into account in the structure prediction of protein structures from sequence data banks.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Convergent Synthesis of Repeating Peptides (Val-X-Leu-Pro-Pro-Pro)₈Adopting a Polyproline II Conformation

et al. 1996

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“…When enzymes adsorb on surfaces, their activity can be greatly affected by their orientation and surface-induced conformational changes. , Moreover, Gtfs have been shown to be more active after adsorption on sHA than uncoated hydroxyapatite (HA), suggesting that interactions between Gtfs and other adsorbed biomolecules are critically important. We note that previous studies have shown that some salivary proteins change in conformation when adsorbed to tooth or apatite surfaces. − Thus, we hypothesize that Gtfs also undergo major conformational changes during binding to saliva-coated apatite surfaces, which influences their subsequent enzymatic activity.…”

Section: Introductionmentioning

confidence: 69%

Surface-Induced Changes in the Conformation and Glucan Production of Glucosyltransferase Adsorbed on Saliva-Coated Hydroxyapatite

et al. 2015

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Glucosyltransferases (Gtfs) from S. mutans play critical roles in the development of virulent oral biofilms associated with dental caries disease. Gtfs adsorbed to the tooth surface produce glucans that promote local microbial colonization and provide an insoluble exopolysaccharides (EPS) matrix that facilitates biofilm initiation. Moreover, agents that inhibit the enzymatic activity of Gtfs in solution often have reduced or no effects on surface-adsorbed Gtfs. This study elucidated the mechanisms responsible for the differences in functionality that GtfB exhibits in solution vs surface-adsorbed. Upon adsorption to planar fused-quartz substrates, GtfB displayed a 37% loss of helices and 36% increase of β-sheets, as determined by circular dichroism (CD) spectroscopy, and surface-induced conformational changes were more severe on substrates modified with CH3- and NH2-terminated self-assembled monolayers. GtfB also underwent substantial conformation changes when adsorbing to hydroxyapatite (HA) microspheres, likely due to electrostatic interactions between negatively charged GtfB and positively charged HA crystal faces. Conformational changes were lessened when HA surfaces were coated with saliva (sHA) prior to GtfB adsorption. Furthermore, GtfB remained highly active on sHA, as determined by in situ attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy, producing glucans that were structurally different than GtfB in solution and known to increase the accumulation and virulence of biofilms. Our data provide the first insight into the structural underpinnings governing Gtf conformation and enzymatic function that occur on tooth surfaces in vivo, which may lead to designing potent new inhibitors and improved strategies to combat the formation of pathogenic oral biofilms.

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Solution and solid-state circular dichroism analyses of a human salivary proline-rich glycoprotein repeating domain and its subfragments

Cited by 2 publications

References 27 publications

Convergent Synthesis of Repeating Peptides (Val-X-Leu-Pro-Pro-Pro)₈Adopting a Polyproline II Conformation

Convergent Synthesis of Repeating Peptides (Val-X-Leu-Pro-Pro-Pro)₈Adopting a Polyproline II Conformation

Surface-Induced Changes in the Conformation and Glucan Production of Glucosyltransferase Adsorbed on Saliva-Coated Hydroxyapatite

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Solution and solid-state circular dichroism analyses of a human salivary proline-rich glycoprotein repeating domain and its subfragments

Cited by 2 publications

References 27 publications

Convergent Synthesis of Repeating Peptides (Val-X-Leu-Pro-Pro-Pro)8Adopting a Polyproline II Conformation

Convergent Synthesis of Repeating Peptides (Val-X-Leu-Pro-Pro-Pro)8Adopting a Polyproline II Conformation

Surface-Induced Changes in the Conformation and Glucan Production of Glucosyltransferase Adsorbed on Saliva-Coated Hydroxyapatite

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Convergent Synthesis of Repeating Peptides (Val-X-Leu-Pro-Pro-Pro)₈Adopting a Polyproline II Conformation

Convergent Synthesis of Repeating Peptides (Val-X-Leu-Pro-Pro-Pro)₈Adopting a Polyproline II Conformation