Cis→Trans Isomerization of Pro7 in Oxytocin Regulates Zn2+ Binding
Ion mobility/mass spectrometry techniques are employed to investigate the binding of Zn 2+ to the nine-residue peptide hormone oxytocin (OT, Cys 1 -Tyr 2 -Ile 3 -Gln 4 -Asn 5 -Cys 6 -Pro 7 -Leu 8 -Gly 9 -NH 2 , having a disulfide bond between Cys 1 and Cys 6 residues). Zn 2+ binding to OT is known t...
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| Veröffentlicht in: | Journal of the American Society for Mass Spectrometry 2016-08, Vol.27 (8), p.1376-1382 |
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| creator | Fuller, Daniel R. Glover, Matthew S. Pierson, Nicholas A. Kim, DoYong Russell, David H. Clemmer, David E. |
| description | Ion mobility/mass spectrometry techniques are employed to investigate the binding of Zn
2+
to the nine-residue peptide hormone oxytocin (OT, Cys
1
-Tyr
2
-Ile
3
-Gln
4
-Asn
5
-Cys
6
-Pro
7
-Leu
8
-Gly
9
-NH
2
, having a disulfide bond between Cys
1
and Cys
6
residues). Zn
2+
binding to OT is known to increase the affinity of OT for its receptor [Pearlmutter, A. F., Soloff, M. S.: Characterization of the metal ion requirement for oxytocin-receptor interaction in rat mammary gland membranes. J. Biol. Chem.
254
, 3899–3906 (1979)]. In the absence of Zn
2+
, we find evidence for two primary OT conformations, which arise because the Cys
6
–Pro
7
peptide bond exists in both the
trans
- and
cis
-configurations. Upon addition of Zn
2+
, we determine binding constants in water of K
A
= 1.43 ± 0.24 and 0.42 ± 0.12 μM
−1
, for the
trans
- and
cis
-configured populations, respectively. The Zn
2+
bound form of OT, having a cross section of Ω = 235 Å
2
, has Pro
7
in the
trans
-configuration, which agrees with a prior report [Wyttenbach, T., Liu, D., Bowers, M. T.: Interactions of the hormone oxytocin with divalent metal ions. J. Am. Chem. Soc.
130
, 5993–6000 (2008)], in which it was proposed that Zn
2+
binds to the peptide ring and is further coordinated by interaction of the C-terminal, Pro
7
-Leu
8
-Gly
9
-NH
2
, tail. The present work shows that the
cis
-configuration of OT isomerizes to the
trans
-configuration upon binding Zn
2+
. In this way, the proline residue regulates Zn
2+
binding to OT and, hence, is important in receptor binding.
Graphical Abstract
ᅟ |
| doi_str_mv | 10.1007/s13361-016-1410-4 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5161230</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1968048463</sourcerecordid><originalsourceid>FETCH-LOGICAL-p1694-e576e3f66b4abbb5939f750506c57ff0f504195931bf02f8d5e920eb0cee52e83</originalsourceid><addsrcrecordid>eNpVkEtKA0EQhhtRTHwcwN2ASxmt6ufMRtD4BCEiunHTzCTdsUPSHbsnoh7AA3hET2JLXOiqfqp-PoqPkD2EQwRQRwkZk1gCyhI5QsnXSB8rVZeIlK3nDJyXwED0yFZKUwBUUKtN0qMKBQdK--Rs4NLXx-d9bHwqrlOYm-jem84FXwRb3MagCueL4etbF0Y53JnJctZ0JhWPnh4Up86PnZ_skA3bzJLZ_Z3b5OHi_H5wVd4ML68HJzflAmXNSyOUNMxK2fKmbVtRs9oqAQLkSChrwQrgWOc1thaorcbC1BRMCyNjBDUV2ybHK-5i2c7NeGR8F5uZXkQ3b-KbDo3T_y_ePelJeNECZTYCGbD_C4jheWlSp6dhGX3-WWMtK-AVlyy36KqVMtlPTPzTAv1jXq_M62xe_5jXnH0Dp1h1Qg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1968048463</pqid></control><display><type>article</type><title>Cis→Trans Isomerization of Pro7 in Oxytocin Regulates Zn2+ Binding</title><source>SpringerLink Journals - AutoHoldings</source><creator>Fuller, Daniel R. ; Glover, Matthew S. ; Pierson, Nicholas A. ; Kim, DoYong ; Russell, David H. ; Clemmer, David E.</creator><creatorcontrib>Fuller, Daniel R. ; Glover, Matthew S. ; Pierson, Nicholas A. ; Kim, DoYong ; Russell, David H. ; Clemmer, David E.</creatorcontrib><description>Ion mobility/mass spectrometry techniques are employed to investigate the binding of Zn
2+
to the nine-residue peptide hormone oxytocin (OT, Cys
1
-Tyr
2
-Ile
3
-Gln
4
-Asn
5
-Cys
6
-Pro
7
-Leu
8
-Gly
9
-NH
2
, having a disulfide bond between Cys
1
and Cys
6
residues). Zn
2+
binding to OT is known to increase the affinity of OT for its receptor [Pearlmutter, A. F., Soloff, M. S.: Characterization of the metal ion requirement for oxytocin-receptor interaction in rat mammary gland membranes. J. Biol. Chem.
254
, 3899–3906 (1979)]. In the absence of Zn
2+
, we find evidence for two primary OT conformations, which arise because the Cys
6
–Pro
7
peptide bond exists in both the
trans
- and
cis
-configurations. Upon addition of Zn
2+
, we determine binding constants in water of K
A
= 1.43 ± 0.24 and 0.42 ± 0.12 μM
−1
, for the
trans
- and
cis
-configured populations, respectively. The Zn
2+
bound form of OT, having a cross section of Ω = 235 Å
2
, has Pro
7
in the
trans
-configuration, which agrees with a prior report [Wyttenbach, T., Liu, D., Bowers, M. T.: Interactions of the hormone oxytocin with divalent metal ions. J. Am. Chem. Soc.
130
, 5993–6000 (2008)], in which it was proposed that Zn
2+
binds to the peptide ring and is further coordinated by interaction of the C-terminal, Pro
7
-Leu
8
-Gly
9
-NH
2
, tail. The present work shows that the
cis
-configuration of OT isomerizes to the
trans
-configuration upon binding Zn
2+
. In this way, the proline residue regulates Zn
2+
binding to OT and, hence, is important in receptor binding.
Graphical Abstract
ᅟ</description><identifier>ISSN: 1044-0305</identifier><identifier>EISSN: 1879-1123</identifier><identifier>DOI: 10.1007/s13361-016-1410-4</identifier><identifier>PMID: 27154022</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Analytical Chemistry ; Binding ; Bioinformatics ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Configurations ; Ionic mobility ; Ions ; Isomerization ; Mass spectrometry ; Metal ions ; Organic Chemistry ; Peptides ; Proline ; Proteomics ; Research Article ; Rodents</subject><ispartof>Journal of the American Society for Mass Spectrometry, 2016-08, Vol.27 (8), p.1376-1382</ispartof><rights>American Society for Mass Spectrometry 2016</rights><rights>Journal of The American Society for Mass Spectrometry is a copyright of Springer, (2016). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-p1694-e576e3f66b4abbb5939f750506c57ff0f504195931bf02f8d5e920eb0cee52e83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s13361-016-1410-4$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s13361-016-1410-4$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,780,784,885,27924,27925,41488,42557,51319</link.rule.ids></links><search><creatorcontrib>Fuller, Daniel R.</creatorcontrib><creatorcontrib>Glover, Matthew S.</creatorcontrib><creatorcontrib>Pierson, Nicholas A.</creatorcontrib><creatorcontrib>Kim, DoYong</creatorcontrib><creatorcontrib>Russell, David H.</creatorcontrib><creatorcontrib>Clemmer, David E.</creatorcontrib><title>Cis→Trans Isomerization of Pro7 in Oxytocin Regulates Zn2+ Binding</title><title>Journal of the American Society for Mass Spectrometry</title><addtitle>J. Am. Soc. Mass Spectrom</addtitle><description>Ion mobility/mass spectrometry techniques are employed to investigate the binding of Zn
2+
to the nine-residue peptide hormone oxytocin (OT, Cys
1
-Tyr
2
-Ile
3
-Gln
4
-Asn
5
-Cys
6
-Pro
7
-Leu
8
-Gly
9
-NH
2
, having a disulfide bond between Cys
1
and Cys
6
residues). Zn
2+
binding to OT is known to increase the affinity of OT for its receptor [Pearlmutter, A. F., Soloff, M. S.: Characterization of the metal ion requirement for oxytocin-receptor interaction in rat mammary gland membranes. J. Biol. Chem.
254
, 3899–3906 (1979)]. In the absence of Zn
2+
, we find evidence for two primary OT conformations, which arise because the Cys
6
–Pro
7
peptide bond exists in both the
trans
- and
cis
-configurations. Upon addition of Zn
2+
, we determine binding constants in water of K
A
= 1.43 ± 0.24 and 0.42 ± 0.12 μM
−1
, for the
trans
- and
cis
-configured populations, respectively. The Zn
2+
bound form of OT, having a cross section of Ω = 235 Å
2
, has Pro
7
in the
trans
-configuration, which agrees with a prior report [Wyttenbach, T., Liu, D., Bowers, M. T.: Interactions of the hormone oxytocin with divalent metal ions. J. Am. Chem. Soc.
130
, 5993–6000 (2008)], in which it was proposed that Zn
2+
binds to the peptide ring and is further coordinated by interaction of the C-terminal, Pro
7
-Leu
8
-Gly
9
-NH
2
, tail. The present work shows that the
cis
-configuration of OT isomerizes to the
trans
-configuration upon binding Zn
2+
. In this way, the proline residue regulates Zn
2+
binding to OT and, hence, is important in receptor binding.
Graphical Abstract
ᅟ</description><subject>Analytical Chemistry</subject><subject>Binding</subject><subject>Bioinformatics</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Configurations</subject><subject>Ionic mobility</subject><subject>Ions</subject><subject>Isomerization</subject><subject>Mass spectrometry</subject><subject>Metal ions</subject><subject>Organic Chemistry</subject><subject>Peptides</subject><subject>Proline</subject><subject>Proteomics</subject><subject>Research Article</subject><subject>Rodents</subject><issn>1044-0305</issn><issn>1879-1123</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpVkEtKA0EQhhtRTHwcwN2ASxmt6ufMRtD4BCEiunHTzCTdsUPSHbsnoh7AA3hET2JLXOiqfqp-PoqPkD2EQwRQRwkZk1gCyhI5QsnXSB8rVZeIlK3nDJyXwED0yFZKUwBUUKtN0qMKBQdK--Rs4NLXx-d9bHwqrlOYm-jem84FXwRb3MagCueL4etbF0Y53JnJctZ0JhWPnh4Up86PnZ_skA3bzJLZ_Z3b5OHi_H5wVd4ML68HJzflAmXNSyOUNMxK2fKmbVtRs9oqAQLkSChrwQrgWOc1thaorcbC1BRMCyNjBDUV2ybHK-5i2c7NeGR8F5uZXkQ3b-KbDo3T_y_ePelJeNECZTYCGbD_C4jheWlSp6dhGX3-WWMtK-AVlyy36KqVMtlPTPzTAv1jXq_M62xe_5jXnH0Dp1h1Qg</recordid><startdate>20160801</startdate><enddate>20160801</enddate><creator>Fuller, Daniel R.</creator><creator>Glover, Matthew S.</creator><creator>Pierson, Nicholas A.</creator><creator>Kim, DoYong</creator><creator>Russell, David H.</creator><creator>Clemmer, David E.</creator><general>Springer US</general><general>Springer Nature B.V</general><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FG</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>5PM</scope></search><sort><creationdate>20160801</creationdate><title>Cis→Trans Isomerization of Pro7 in Oxytocin Regulates Zn2+ Binding</title><author>Fuller, Daniel R. ; Glover, Matthew S. ; Pierson, Nicholas A. ; Kim, DoYong ; Russell, David H. ; Clemmer, David E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p1694-e576e3f66b4abbb5939f750506c57ff0f504195931bf02f8d5e920eb0cee52e83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Analytical Chemistry</topic><topic>Binding</topic><topic>Bioinformatics</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Configurations</topic><topic>Ionic mobility</topic><topic>Ions</topic><topic>Isomerization</topic><topic>Mass spectrometry</topic><topic>Metal ions</topic><topic>Organic Chemistry</topic><topic>Peptides</topic><topic>Proline</topic><topic>Proteomics</topic><topic>Research Article</topic><topic>Rodents</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fuller, Daniel R.</creatorcontrib><creatorcontrib>Glover, Matthew S.</creatorcontrib><creatorcontrib>Pierson, Nicholas A.</creatorcontrib><creatorcontrib>Kim, DoYong</creatorcontrib><creatorcontrib>Russell, David H.</creatorcontrib><creatorcontrib>Clemmer, David E.</creatorcontrib><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of the American Society for Mass Spectrometry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fuller, Daniel R.</au><au>Glover, Matthew S.</au><au>Pierson, Nicholas A.</au><au>Kim, DoYong</au><au>Russell, David H.</au><au>Clemmer, David E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cis→Trans Isomerization of Pro7 in Oxytocin Regulates Zn2+ Binding</atitle><jtitle>Journal of the American Society for Mass Spectrometry</jtitle><stitle>J. Am. Soc. Mass Spectrom</stitle><date>2016-08-01</date><risdate>2016</risdate><volume>27</volume><issue>8</issue><spage>1376</spage><epage>1382</epage><pages>1376-1382</pages><issn>1044-0305</issn><eissn>1879-1123</eissn><abstract>Ion mobility/mass spectrometry techniques are employed to investigate the binding of Zn
2+
to the nine-residue peptide hormone oxytocin (OT, Cys
1
-Tyr
2
-Ile
3
-Gln
4
-Asn
5
-Cys
6
-Pro
7
-Leu
8
-Gly
9
-NH
2
, having a disulfide bond between Cys
1
and Cys
6
residues). Zn
2+
binding to OT is known to increase the affinity of OT for its receptor [Pearlmutter, A. F., Soloff, M. S.: Characterization of the metal ion requirement for oxytocin-receptor interaction in rat mammary gland membranes. J. Biol. Chem.
254
, 3899–3906 (1979)]. In the absence of Zn
2+
, we find evidence for two primary OT conformations, which arise because the Cys
6
–Pro
7
peptide bond exists in both the
trans
- and
cis
-configurations. Upon addition of Zn
2+
, we determine binding constants in water of K
A
= 1.43 ± 0.24 and 0.42 ± 0.12 μM
−1
, for the
trans
- and
cis
-configured populations, respectively. The Zn
2+
bound form of OT, having a cross section of Ω = 235 Å
2
, has Pro
7
in the
trans
-configuration, which agrees with a prior report [Wyttenbach, T., Liu, D., Bowers, M. T.: Interactions of the hormone oxytocin with divalent metal ions. J. Am. Chem. Soc.
130
, 5993–6000 (2008)], in which it was proposed that Zn
2+
binds to the peptide ring and is further coordinated by interaction of the C-terminal, Pro
7
-Leu
8
-Gly
9
-NH
2
, tail. The present work shows that the
cis
-configuration of OT isomerizes to the
trans
-configuration upon binding Zn
2+
. In this way, the proline residue regulates Zn
2+
binding to OT and, hence, is important in receptor binding.
Graphical Abstract
ᅟ</abstract><cop>New York</cop><pub>Springer US</pub><pmid>27154022</pmid><doi>10.1007/s13361-016-1410-4</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| source | SpringerLink Journals - AutoHoldings |
| subjects | Analytical Chemistry Binding Bioinformatics Biotechnology Chemistry Chemistry and Materials Science Configurations Ionic mobility Ions Isomerization Mass spectrometry Metal ions Organic Chemistry Peptides Proline Proteomics Research Article Rodents |
| title | Cis→Trans Isomerization of Pro7 in Oxytocin Regulates Zn2+ Binding |
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