Soft-landing of peptide ions onto self-assembled monolayer surfaces: an overview

Laskin, Julia; Wang, Peng; Hadjar, Omar

doi:10.1039/b712710c

Cited by 115 publications

(184 citation statements)

References 79 publications

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“…This potential accurately describes the short-range, repulsive interactions which determine the collisional energy-transfer, but not the longrange intermolecular potential. The latter describes the attractive interaction of the peptide ion with the surface and is necessary to model soft-landing experiments [23,24] in which the ion binds to the surface. Work has been done to develop these potentials [25].…”

Section: Potential Energy Functionmentioning

confidence: 99%

Importance of shattering fragmentation in the surface-induced dissociation of protonated octaglycine

Park

Deb

Song

et al. 2009

J. Am. Soc. Mass Spectrom.

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A QM ϩ MM direct chemical dynamics simulation was performed to study collisions of protonated octaglycine, gly 8 -H ϩ , with the diamond {111} surface at an initial collision energy E i of 100 eV and incident angle i of 0°and 45°. The semiempirical model AM1 was used for the gly 8 -H ϩ intramolecular potential, so that its fragmentation could be studied. Shattering dominates gly 8 -H ϩ fragmentation at i ϭ 0°, with 78% of the ions dissociating in this way. At i ϭ 45°shattering is much less important. For i ϭ 0°there are 304 different pathways, many related by their backbone cleavage patterns. For the i ϭ 0°fragmentations, 59% resulted from both a-x and b-y cleavages, while for i ϭ 45°70% of the fragmentations occurred with only a-x cleavage. For i ϭ 0°, the average percentage energy transfers to the internal degrees of freedom of the ion and the surface, and the energy remaining in ion translation are 45%, 26%, and 29%. For 45°these percentages are 26%, 12%, and 62%. The percentage energy-transfer to ⌬E int for i ϭ 0°is larger than that reported in previous experiments for collisions of des-Arg 1 -bradykinin with a diamond surface at the same i . This difference is discussed in terms of differences between the model diamond surface used in the simulations and the diamond surface prepared for the experiments. (J Am Soc Mass Spectrom 2009, 20, 939 -948)

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Section: Potential Energy Functionmentioning

confidence: 99%

Importance of shattering fragmentation in the surface-induced dissociation of protonated octaglycine

Park

Deb

Song

et al. 2009

J. Am. Soc. Mass Spectrom.

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“…Gas phase separation of isomeric species has also been achieved through ion mobility techniques (19), which could be used as a further purification method. Furthermore, methods for collecting peptides and proteins in the gas phase have been developed based on softlanding techniques (20)(21)(22), which have even been extended to create microarrays of protein ions (23) from a mass spectrometer. By activating the carboxyl group of amino acids or peptides with NHS or sulfoNHS esters and protecting reactive functionalities, such as the amines, with gas phase-labile protecting groups, we generate a reagent that can be covalently attached to the N terminus of an existing unprotected peptide, which we call the "anchor" peptide.…”

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confidence: 99%

Efficient and directed peptide bond formation in the gas phase via ion/ion reactions

McGee

McLuckey

2014

Proc. Natl. Acad. Sci. U.S.A.

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Amide linkages are among the most important chemical bonds in living systems, constituting the connections between amino acids in peptides and proteins. We demonstrate the controlled formation of amide bonds between amino acids or peptides in the gas phase using ion/ion reactions in a mass spectrometer. Individual amino acids or peptides can be prepared as reagents by (i) incorporating gas phaselabile protecting groups to silence otherwise reactive functional groups, such as the N terminus; (ii) converting the carboxyl groups to the active ester of N-hydroxysuccinimide; and (iii) incorporating a charge site. Protonation renders basic sites (nucleophiles) unreactive toward the N-hydroxysuccinimide ester reagents, resulting in sites with the greatest gas phase basicities being, in large part, unreactive. The N-terminal amines of most naturally occurring amino acids have lower gas phase basicities than the side chains of the basic amino acids (i.e., those of histidine, lysine, or arginine). Therefore, reagents may be directed to the N terminus of an existing "anchor" peptide to form an amide bond by protonating the anchor peptide's basic residues, while leaving the N-terminal amine unprotonated and therefore reactive. Reaction efficiencies of greater than 30% have been observed. We propose this method as a step toward the controlled synthesis of peptides in the gas phase.peptide ligation | ion chemistry T he formation of amide bonds between amino acids holds widespread interest as it is relevant to the origin of life. Although the process by which these early peptides were formed remains an open question, laboratory-based approaches for peptide synthesis have been in place for over a century. The first controlled synthesis of diglycine via hydrolysis of diketopiperazine by Fisher in 1901 (1) marked the beginning of a long path of development of peptide synthesis approaches. Since that time, peptide synthesis has undergone several developments, beginning as solution phase reactions and eventually evolving in 1963 with Merrifield's introduction of solid resins in peptide synthesis (2), more commonly referred to as solid phase peptide synthesis (SPPS). Although this technique has undergone a dynamic maturation over the past few decades, it is still regarded as expensive and inelegant (3, 4). Furthermore, there are still several challenges that are not likely to be overcome without a significant change to the synthesis approach, beyond inherent challenges such as, for example, solubility of reagents. SPPS requires significant use of protecting and deprotecting agents, cleaving agents, and other solvents for washing, drying, and dissolving the newly formed peptides. This method quickly becomes a rather wasteful approach when considering the sacrifices made to produce just a single amide bond (3). Alternative synthesis approaches, such as chemical ligation (5, 6) and molecular machine-mediated peptide synthesis (7), offer more elegant approaches despite maintaining several of the previously mentioned requirements.Amide b...

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“…For example, protein adsorption on substrates is a highly dynamic process that is strongly influenced by Coulomb interactions, hydrogen bonding, and relatively weak noncovalent interactions. These processes are highly dependant on the primary and the highorder structure of the protein and on the properties of the surface and the solvent.It has recently been demonstrated that soft-landing (SL) of mass-selected ions on surfaces is a useful mass spectrometric approach for probing details of this intrinsic behavior of immobilized biological molecules that removes the strong effects of solvents [3][4][5]. SL is defined as intact capture of mass-selected polyatomic ions on substrates [6,7] and has already been successfully used to study charge retention by small closedshell ions [6 -9] and peptide and protein ions deposited onto self-assembled monolayer surfaces (SAMs) [10 -13].…”

mentioning

confidence: 99%

Effect of the surface on charge reduction and desorption kinetics of soft landed peptide ions

Hadjar

Wang

Laskin

2009

J. Am. Soc. Mass Spectrom.

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Charge reduction and desorption kinetics of ions and neutral molecules produced by soft-landing of mass-selected singly and doubly protonated Gramicidin S (GS) on different surfaces was studied using time dependant in situ secondary ion mass spectrometry (SIMS) integrated in a specially designed Fourier transform ion cyclotron resonance mass spectrometer (FT-ICR MS) research instrument. Soft-landing targets utilized in this study included inert self-assembled monolayers (SAMs) of 1-dodecane thiol (HSAM) and its fluorinated analog (FSAM) on gold and hydrophilic carboxyl-terminated (COOH-SAM) and amine-terminated (NH 2 -SAM) surfaces. We observed efficient neutralization of soft-landed ions on the COOH-SAM surface, partial retention of only one proton on the HSAM surface, and efficient retention of two protons on the FSAM surface. For example, protein adsorption on substrates is a highly dynamic process that is strongly influenced by Coulomb interactions, hydrogen bonding, and relatively weak noncovalent interactions. These processes are highly dependant on the primary and the highorder structure of the protein and on the properties of the surface and the solvent.It has recently been demonstrated that soft-landing (SL) of mass-selected ions on surfaces is a useful mass spectrometric approach for probing details of this intrinsic behavior of immobilized biological molecules that removes the strong effects of solvents [3][4][5]. SL is defined as intact capture of mass-selected polyatomic ions on substrates [6,7] and has already been successfully used to study charge retention by small closedshell ions [6 -9] and peptide and protein ions deposited onto self-assembled monolayer surfaces (SAMs) [10 -13]. Retention of biological activity (but not charge) by proteins deposited on liquid [10,14] and on plasma treated metal surfaces [15] has also been demonstrated.Recently we reported the first detailed study of the kinetics of desorption and charge reduction following SL of doubly protonated Gramicidin S (GS) onto the FSAM surface [16]. We utilized an in-line 8 keV Cs ϩ ion gun that allowed us to interrogate the surface in situ and in real time using secondary ion mass spectrometry (SIMS). We followed the evolution of the SIMS spectrum as a function of time during and after the deposition of [GS ϩ 2H] 2ϩ and obtained unique kinetics signatures for doubly protonated, singly protonated, and neutral peptides retained on the surface. Using the characteristic ion signatures and a kinetic model we measured rate coefficients for charge reduction and thermal desorption of ions and neutral GS molecules from the surface. An important process established in that work was the instantaneous loss of one or two protons by a fraction of ions colliding with the FSAM surface. Collision induced fast charge reduction is followed by very slow proton loss by ions trapped on the surface. Thermal desorption of ionic and neutral species efficiently competes with the charge reduction process.In this research, we applied the same in situ SIMS tec...

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Soft-landing of peptide ions onto self-assembled monolayer surfaces: an overview

Cited by 115 publications

References 79 publications

Importance of shattering fragmentation in the surface-induced dissociation of protonated octaglycine

Importance of shattering fragmentation in the surface-induced dissociation of protonated octaglycine

Efficient and directed peptide bond formation in the gas phase via ion/ion reactions

Effect of the surface on charge reduction and desorption kinetics of soft landed peptide ions

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