Stabilization of compact protein structures by macrocyclic hosts cucurbit[n]urils in the gas phase

Jong Wha Lee, Mi Hyun Park, Jeong Tae Ju, Yun Seop Choi, Soo Min Hwang, Dong Jin Jung, Hugh I. Kim

Research output: Contribution to journalLetter

2 Citations (Scopus)

Abstract

Characterization of intact protein structures in the gas phase using electrospray ionization combined with ion mobility mass spectrometry has become an important tool of research. However, the biophysical properties that govern the structures of protein ions in the gas phase remain to be understood. Here, we investigated the impact of host-guest complexation of ubiquitin (Ubq) with macrocyclic host molecules, cucurbit[n]urils (CB[n]s, n = 6, 7), on its structure in the gas phase. We found that CB[n] complexation induces the formation of compact Ubq ions. Both CB[6] and CB[7] exhibited similar effects despite differences in their binding properties in solution. In addition, CB[n] attachment prevented Ubq from unfolding by collisional activation. Based on the experimental results, we suggest that CB[n]s prevent unfolding of Ubq during transfer to the gas phase to promote the formation of compact protein ions. Furthermore, interaction with positively charged residues per se is suggested to be the most important factor for the host-guest complexation effect.

Original languageEnglish
Pages (from-to)16-20
Number of pages5
JournalMass Spectrometry Letters
Volume7
Issue number1
DOIs
Publication statusPublished - 2016 Mar 1

Fingerprint

Ubiquitin
Stabilization
Gases
Complexation
Ions
Proteins
Electrospray ionization
Mass spectrometry
Mass Spectrometry
Chemical activation
Molecules
Research

Keywords

  • Cucurbit[n]uril
  • Host-guest chemistry
  • Ion mobility mass spectrometry
  • Ubiquitin

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Spectroscopy

Cite this

Stabilization of compact protein structures by macrocyclic hosts cucurbit[n]urils in the gas phase. / Lee, Jong Wha; Park, Mi Hyun; Ju, Jeong Tae; Choi, Yun Seop; Hwang, Soo Min; Jung, Dong Jin; Kim, Hugh I.

In: Mass Spectrometry Letters, Vol. 7, No. 1, 01.03.2016, p. 16-20.

Research output: Contribution to journalLetter

Lee, Jong Wha ; Park, Mi Hyun ; Ju, Jeong Tae ; Choi, Yun Seop ; Hwang, Soo Min ; Jung, Dong Jin ; Kim, Hugh I. / Stabilization of compact protein structures by macrocyclic hosts cucurbit[n]urils in the gas phase. In: Mass Spectrometry Letters. 2016 ; Vol. 7, No. 1. pp. 16-20.
@article{607a710b37bc42e1bb4856c613a5f6bc,
title = "Stabilization of compact protein structures by macrocyclic hosts cucurbit[n]urils in the gas phase",
abstract = "Characterization of intact protein structures in the gas phase using electrospray ionization combined with ion mobility mass spectrometry has become an important tool of research. However, the biophysical properties that govern the structures of protein ions in the gas phase remain to be understood. Here, we investigated the impact of host-guest complexation of ubiquitin (Ubq) with macrocyclic host molecules, cucurbit[n]urils (CB[n]s, n = 6, 7), on its structure in the gas phase. We found that CB[n] complexation induces the formation of compact Ubq ions. Both CB[6] and CB[7] exhibited similar effects despite differences in their binding properties in solution. In addition, CB[n] attachment prevented Ubq from unfolding by collisional activation. Based on the experimental results, we suggest that CB[n]s prevent unfolding of Ubq during transfer to the gas phase to promote the formation of compact protein ions. Furthermore, interaction with positively charged residues per se is suggested to be the most important factor for the host-guest complexation effect.",
keywords = "Cucurbit[n]uril, Host-guest chemistry, Ion mobility mass spectrometry, Ubiquitin",
author = "Lee, {Jong Wha} and Park, {Mi Hyun} and Ju, {Jeong Tae} and Choi, {Yun Seop} and Hwang, {Soo Min} and Jung, {Dong Jin} and Kim, {Hugh I.}",
year = "2016",
month = "3",
day = "1",
doi = "10.5478/MSL.2016.7.1.16",
language = "English",
volume = "7",
pages = "16--20",
journal = "Mass Spectrometry Letters",
issn = "2233-4203",
publisher = "Korean Society Mass Spectrometry",
number = "1",

}

TY - JOUR

T1 - Stabilization of compact protein structures by macrocyclic hosts cucurbit[n]urils in the gas phase

AU - Lee, Jong Wha

AU - Park, Mi Hyun

AU - Ju, Jeong Tae

AU - Choi, Yun Seop

AU - Hwang, Soo Min

AU - Jung, Dong Jin

AU - Kim, Hugh I.

PY - 2016/3/1

Y1 - 2016/3/1

N2 - Characterization of intact protein structures in the gas phase using electrospray ionization combined with ion mobility mass spectrometry has become an important tool of research. However, the biophysical properties that govern the structures of protein ions in the gas phase remain to be understood. Here, we investigated the impact of host-guest complexation of ubiquitin (Ubq) with macrocyclic host molecules, cucurbit[n]urils (CB[n]s, n = 6, 7), on its structure in the gas phase. We found that CB[n] complexation induces the formation of compact Ubq ions. Both CB[6] and CB[7] exhibited similar effects despite differences in their binding properties in solution. In addition, CB[n] attachment prevented Ubq from unfolding by collisional activation. Based on the experimental results, we suggest that CB[n]s prevent unfolding of Ubq during transfer to the gas phase to promote the formation of compact protein ions. Furthermore, interaction with positively charged residues per se is suggested to be the most important factor for the host-guest complexation effect.

AB - Characterization of intact protein structures in the gas phase using electrospray ionization combined with ion mobility mass spectrometry has become an important tool of research. However, the biophysical properties that govern the structures of protein ions in the gas phase remain to be understood. Here, we investigated the impact of host-guest complexation of ubiquitin (Ubq) with macrocyclic host molecules, cucurbit[n]urils (CB[n]s, n = 6, 7), on its structure in the gas phase. We found that CB[n] complexation induces the formation of compact Ubq ions. Both CB[6] and CB[7] exhibited similar effects despite differences in their binding properties in solution. In addition, CB[n] attachment prevented Ubq from unfolding by collisional activation. Based on the experimental results, we suggest that CB[n]s prevent unfolding of Ubq during transfer to the gas phase to promote the formation of compact protein ions. Furthermore, interaction with positively charged residues per se is suggested to be the most important factor for the host-guest complexation effect.

KW - Cucurbit[n]uril

KW - Host-guest chemistry

KW - Ion mobility mass spectrometry

KW - Ubiquitin

UR - http://www.scopus.com/inward/record.url?scp=84963502496&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84963502496&partnerID=8YFLogxK

U2 - 10.5478/MSL.2016.7.1.16

DO - 10.5478/MSL.2016.7.1.16

M3 - Letter

AN - SCOPUS:84963502496

VL - 7

SP - 16

EP - 20

JO - Mass Spectrometry Letters

JF - Mass Spectrometry Letters

SN - 2233-4203

IS - 1

ER -