Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent
Alyteserin-2a (ILGKLLSTAAGLLSNL.NH 2 ) is a cationic, amphipathic α-helical cell-penetrating peptide, first isolated from skin secretions of the midwife toad Alytes obstetricans . Structure–activity relationships were investigated by synthesizing analogs of alyteserin-2a in which amino acids on the...
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| creator | Conlon, J. Michael Mechkarska, Milena Prajeep, Manju Arafat, Kholoud Zaric, Milan Lukic, Miodrag L. Attoub, Samir |
| description | Alyteserin-2a (ILGKLLSTAAGLLSNL.NH
2
) is a cationic, amphipathic α-helical cell-penetrating peptide, first isolated from skin secretions of the midwife toad
Alytes obstetricans
. Structure–activity relationships were investigated by synthesizing analogs of alyteserin-2a in which amino acids on the hydrophobic face of the helix were replaced by
l
-tryptophan and amino acids on the hydrophilic face were replaced by one or more
l
-lysine or
d
-lysine residues. The Trp-containing peptides display increased cytotoxic activity against non-small cell lung adenocarcinoma A549 cells (up to 11-fold), but hemolytic activity against human erythrocytes increases in parallel. The potency of the N15K analog against A549 cells (LC
50
= 13 μM) increases sixfold relative to alyteserin-2a and the therapeutic index (ratio of LC
50
for erythrocytes and tumor cells) increases twofold. Incorporation of a
d
-Lys
11
residue into the N15K analog generates a peptide that retains potency against A549 cells (LC
50
= 15 μM) but whose therapeutic index is 13-fold elevated relative to the native peptide. [G11k, N15K] alyteserin-2a is also active against human hepatocarcinoma HepG2 cells (LC
50
= 26 μM), breast adenocarcinoma MDA-MB-231 cells (LC
50
= 20 μM), and colorectal adenocarcinoma HT-29 cells (LC
50
= 28 μM). [G11k, N15K] alyteserin-2a, in concentrations as low as 1 μg/mL, significantly (
P
|
| doi_str_mv | 10.1007/s00726-012-1395-7 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1315687602</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2871328091</sourcerecordid><originalsourceid>FETCH-LOGICAL-c405t-b4825e3834da9ae7f1348fc134454814673360b296b8b0c51a4fd6516ffc95233</originalsourceid><addsrcrecordid>eNp1kctuFDEQRS1ERIbAB7BBltiwiIPLr3YvUcRLisQmWVtujz049NiN7ZYyfx-PJiCExKZqUaduPS5Cb4BeAaXDh9oDU4QCI8BHSYZnaAOCa8JgHJ-jDR35SISQcI5e1npPO6hBvUDnjI1KKj5s0HpbbKohl71tMSecA24_PE62rcXO8wFn59ZSYtrhUPIO158x4cUvLW79Jbbzofnqe5kwi2NqGVu85OZTu8QpJ9LyQ3TYphaJs8n5gu2uF1-hs2Dn6l8_5Qt09_nT7fVXcvP9y7frjzfECSobmYRm0nPNxdaO1g8BuNDB9Sik0CDUwLmiUz9m0hN1EqwIWyVBheBGyTi_QO9PukvJv1Zfm9nH6vw82-TzWg1wkEoPirKOvvsHvc9rSX07A2wArSlXslNwolzJtRYfzFLi3paDAWqOnpiTJ6a_2hw9MUPvefukvE57v_3T8duEDrATUJfjo335a_R_VR8Br5WWgg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1271880365</pqid></control><display><type>article</type><title>Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><creator>Conlon, J. Michael ; Mechkarska, Milena ; Prajeep, Manju ; Arafat, Kholoud ; Zaric, Milan ; Lukic, Miodrag L. ; Attoub, Samir</creator><creatorcontrib>Conlon, J. Michael ; Mechkarska, Milena ; Prajeep, Manju ; Arafat, Kholoud ; Zaric, Milan ; Lukic, Miodrag L. ; Attoub, Samir</creatorcontrib><description>Alyteserin-2a (ILGKLLSTAAGLLSNL.NH
2
) is a cationic, amphipathic α-helical cell-penetrating peptide, first isolated from skin secretions of the midwife toad
Alytes obstetricans
. Structure–activity relationships were investigated by synthesizing analogs of alyteserin-2a in which amino acids on the hydrophobic face of the helix were replaced by
l
-tryptophan and amino acids on the hydrophilic face were replaced by one or more
l
-lysine or
d
-lysine residues. The Trp-containing peptides display increased cytotoxic activity against non-small cell lung adenocarcinoma A549 cells (up to 11-fold), but hemolytic activity against human erythrocytes increases in parallel. The potency of the N15K analog against A549 cells (LC
50
= 13 μM) increases sixfold relative to alyteserin-2a and the therapeutic index (ratio of LC
50
for erythrocytes and tumor cells) increases twofold. Incorporation of a
d
-Lys
11
residue into the N15K analog generates a peptide that retains potency against A549 cells (LC
50
= 15 μM) but whose therapeutic index is 13-fold elevated relative to the native peptide. [G11k, N15K] alyteserin-2a is also active against human hepatocarcinoma HepG2 cells (LC
50
= 26 μM), breast adenocarcinoma MDA-MB-231 cells (LC
50
= 20 μM), and colorectal adenocarcinoma HT-29 cells (LC
50
= 28 μM). [G11k, N15K] alyteserin-2a, in concentrations as low as 1 μg/mL, significantly (
P
< 0.05) inhibits the release of the immune-suppressive cytokines IL-10 and TGF-β from unstimulated and concanavalin A-stimulated peripheral blood mononuclear cells. The data suggest a strategy of increasing the cationicity while reducing the helicity of naturally occurring amphipathic α-helical peptides to generate analogs with improved cytotoxicity against tumor cells but decreased activity against non-neoplastic cells.</description><identifier>ISSN: 0939-4451</identifier><identifier>EISSN: 1438-2199</identifier><identifier>DOI: 10.1007/s00726-012-1395-7</identifier><identifier>PMID: 22965637</identifier><language>eng</language><publisher>Vienna: Springer Vienna</publisher><subject>Alytes obstetricans ; Amino Acid Sequence ; Amphibia ; Analytical Chemistry ; Animals ; Antimicrobial Cationic Peptides - chemical synthesis ; Antimicrobial Cationic Peptides - chemistry ; Antimicrobial Cationic Peptides - pharmacology ; Antineoplastic Agents - chemical synthesis ; Antineoplastic Agents - chemistry ; Antineoplastic Agents - pharmacology ; Anura ; Anura - metabolism ; Biochemical Engineering ; Biochemistry ; Biomedical and Life Sciences ; Cell Line, Tumor ; HT29 Cells ; Humans ; Life Sciences ; Molecular Sequence Data ; Neoplasms - drug therapy ; Neurobiology ; Original Article ; Proteomics ; Skin - chemistry ; Skin - metabolism ; Structure-Activity Relationship</subject><ispartof>Amino acids, 2013-02, Vol.44 (2), p.715-723</ispartof><rights>Springer-Verlag 2012</rights><rights>Springer-Verlag Wien 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-b4825e3834da9ae7f1348fc134454814673360b296b8b0c51a4fd6516ffc95233</citedby><cites>FETCH-LOGICAL-c405t-b4825e3834da9ae7f1348fc134454814673360b296b8b0c51a4fd6516ffc95233</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/s00726-012-1395-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00726-012-1395-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,778,782,27907,27908,41471,42540,51302</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22965637$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Conlon, J. Michael</creatorcontrib><creatorcontrib>Mechkarska, Milena</creatorcontrib><creatorcontrib>Prajeep, Manju</creatorcontrib><creatorcontrib>Arafat, Kholoud</creatorcontrib><creatorcontrib>Zaric, Milan</creatorcontrib><creatorcontrib>Lukic, Miodrag L.</creatorcontrib><creatorcontrib>Attoub, Samir</creatorcontrib><title>Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent</title><title>Amino acids</title><addtitle>Amino Acids</addtitle><addtitle>Amino Acids</addtitle><description>Alyteserin-2a (ILGKLLSTAAGLLSNL.NH
2
) is a cationic, amphipathic α-helical cell-penetrating peptide, first isolated from skin secretions of the midwife toad
Alytes obstetricans
. Structure–activity relationships were investigated by synthesizing analogs of alyteserin-2a in which amino acids on the hydrophobic face of the helix were replaced by
l
-tryptophan and amino acids on the hydrophilic face were replaced by one or more
l
-lysine or
d
-lysine residues. The Trp-containing peptides display increased cytotoxic activity against non-small cell lung adenocarcinoma A549 cells (up to 11-fold), but hemolytic activity against human erythrocytes increases in parallel. The potency of the N15K analog against A549 cells (LC
50
= 13 μM) increases sixfold relative to alyteserin-2a and the therapeutic index (ratio of LC
50
for erythrocytes and tumor cells) increases twofold. Incorporation of a
d
-Lys
11
residue into the N15K analog generates a peptide that retains potency against A549 cells (LC
50
= 15 μM) but whose therapeutic index is 13-fold elevated relative to the native peptide. [G11k, N15K] alyteserin-2a is also active against human hepatocarcinoma HepG2 cells (LC
50
= 26 μM), breast adenocarcinoma MDA-MB-231 cells (LC
50
= 20 μM), and colorectal adenocarcinoma HT-29 cells (LC
50
= 28 μM). [G11k, N15K] alyteserin-2a, in concentrations as low as 1 μg/mL, significantly (
P
< 0.05) inhibits the release of the immune-suppressive cytokines IL-10 and TGF-β from unstimulated and concanavalin A-stimulated peripheral blood mononuclear cells. The data suggest a strategy of increasing the cationicity while reducing the helicity of naturally occurring amphipathic α-helical peptides to generate analogs with improved cytotoxicity against tumor cells but decreased activity against non-neoplastic cells.</description><subject>Alytes obstetricans</subject><subject>Amino Acid Sequence</subject><subject>Amphibia</subject><subject>Analytical Chemistry</subject><subject>Animals</subject><subject>Antimicrobial Cationic Peptides - chemical synthesis</subject><subject>Antimicrobial Cationic Peptides - chemistry</subject><subject>Antimicrobial Cationic Peptides - pharmacology</subject><subject>Antineoplastic Agents - chemical synthesis</subject><subject>Antineoplastic Agents - chemistry</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>Anura</subject><subject>Anura - metabolism</subject><subject>Biochemical Engineering</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Line, Tumor</subject><subject>HT29 Cells</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Molecular Sequence Data</subject><subject>Neoplasms - drug therapy</subject><subject>Neurobiology</subject><subject>Original Article</subject><subject>Proteomics</subject><subject>Skin - chemistry</subject><subject>Skin - metabolism</subject><subject>Structure-Activity Relationship</subject><issn>0939-4451</issn><issn>1438-2199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kctuFDEQRS1ERIbAB7BBltiwiIPLr3YvUcRLisQmWVtujz049NiN7ZYyfx-PJiCExKZqUaduPS5Cb4BeAaXDh9oDU4QCI8BHSYZnaAOCa8JgHJ-jDR35SISQcI5e1npPO6hBvUDnjI1KKj5s0HpbbKohl71tMSecA24_PE62rcXO8wFn59ZSYtrhUPIO158x4cUvLW79Jbbzofnqe5kwi2NqGVu85OZTu8QpJ9LyQ3TYphaJs8n5gu2uF1-hs2Dn6l8_5Qt09_nT7fVXcvP9y7frjzfECSobmYRm0nPNxdaO1g8BuNDB9Sik0CDUwLmiUz9m0hN1EqwIWyVBheBGyTi_QO9PukvJv1Zfm9nH6vw82-TzWg1wkEoPirKOvvsHvc9rSX07A2wArSlXslNwolzJtRYfzFLi3paDAWqOnpiTJ6a_2hw9MUPvefukvE57v_3T8duEDrATUJfjo335a_R_VR8Br5WWgg</recordid><startdate>20130201</startdate><enddate>20130201</enddate><creator>Conlon, J. Michael</creator><creator>Mechkarska, Milena</creator><creator>Prajeep, Manju</creator><creator>Arafat, Kholoud</creator><creator>Zaric, Milan</creator><creator>Lukic, Miodrag L.</creator><creator>Attoub, Samir</creator><general>Springer Vienna</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7U7</scope><scope>C1K</scope></search><sort><creationdate>20130201</creationdate><title>Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent</title><author>Conlon, J. Michael ; Mechkarska, Milena ; Prajeep, Manju ; Arafat, Kholoud ; Zaric, Milan ; Lukic, Miodrag L. ; Attoub, Samir</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c405t-b4825e3834da9ae7f1348fc134454814673360b296b8b0c51a4fd6516ffc95233</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Alytes obstetricans</topic><topic>Amino Acid Sequence</topic><topic>Amphibia</topic><topic>Analytical Chemistry</topic><topic>Animals</topic><topic>Antimicrobial Cationic Peptides - chemical synthesis</topic><topic>Antimicrobial Cationic Peptides - chemistry</topic><topic>Antimicrobial Cationic Peptides - pharmacology</topic><topic>Antineoplastic Agents - chemical synthesis</topic><topic>Antineoplastic Agents - chemistry</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>Anura</topic><topic>Anura - metabolism</topic><topic>Biochemical Engineering</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cell Line, Tumor</topic><topic>HT29 Cells</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Molecular Sequence Data</topic><topic>Neoplasms - drug therapy</topic><topic>Neurobiology</topic><topic>Original Article</topic><topic>Proteomics</topic><topic>Skin - chemistry</topic><topic>Skin - metabolism</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Conlon, J. Michael</creatorcontrib><creatorcontrib>Mechkarska, Milena</creatorcontrib><creatorcontrib>Prajeep, Manju</creatorcontrib><creatorcontrib>Arafat, Kholoud</creatorcontrib><creatorcontrib>Zaric, Milan</creatorcontrib><creatorcontrib>Lukic, Miodrag L.</creatorcontrib><creatorcontrib>Attoub, Samir</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection (ProQuest)</collection><collection>Natural Science Collection (ProQuest)</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</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>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Materials Science 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>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Amino acids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Conlon, J. Michael</au><au>Mechkarska, Milena</au><au>Prajeep, Manju</au><au>Arafat, Kholoud</au><au>Zaric, Milan</au><au>Lukic, Miodrag L.</au><au>Attoub, Samir</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent</atitle><jtitle>Amino acids</jtitle><stitle>Amino Acids</stitle><addtitle>Amino Acids</addtitle><date>2013-02-01</date><risdate>2013</risdate><volume>44</volume><issue>2</issue><spage>715</spage><epage>723</epage><pages>715-723</pages><issn>0939-4451</issn><eissn>1438-2199</eissn><abstract>Alyteserin-2a (ILGKLLSTAAGLLSNL.NH
2
) is a cationic, amphipathic α-helical cell-penetrating peptide, first isolated from skin secretions of the midwife toad
Alytes obstetricans
. Structure–activity relationships were investigated by synthesizing analogs of alyteserin-2a in which amino acids on the hydrophobic face of the helix were replaced by
l
-tryptophan and amino acids on the hydrophilic face were replaced by one or more
l
-lysine or
d
-lysine residues. The Trp-containing peptides display increased cytotoxic activity against non-small cell lung adenocarcinoma A549 cells (up to 11-fold), but hemolytic activity against human erythrocytes increases in parallel. The potency of the N15K analog against A549 cells (LC
50
= 13 μM) increases sixfold relative to alyteserin-2a and the therapeutic index (ratio of LC
50
for erythrocytes and tumor cells) increases twofold. Incorporation of a
d
-Lys
11
residue into the N15K analog generates a peptide that retains potency against A549 cells (LC
50
= 15 μM) but whose therapeutic index is 13-fold elevated relative to the native peptide. [G11k, N15K] alyteserin-2a is also active against human hepatocarcinoma HepG2 cells (LC
50
= 26 μM), breast adenocarcinoma MDA-MB-231 cells (LC
50
= 20 μM), and colorectal adenocarcinoma HT-29 cells (LC
50
= 28 μM). [G11k, N15K] alyteserin-2a, in concentrations as low as 1 μg/mL, significantly (
P
< 0.05) inhibits the release of the immune-suppressive cytokines IL-10 and TGF-β from unstimulated and concanavalin A-stimulated peripheral blood mononuclear cells. The data suggest a strategy of increasing the cationicity while reducing the helicity of naturally occurring amphipathic α-helical peptides to generate analogs with improved cytotoxicity against tumor cells but decreased activity against non-neoplastic cells.</abstract><cop>Vienna</cop><pub>Springer Vienna</pub><pmid>22965637</pmid><doi>10.1007/s00726-012-1395-7</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Amino acids, 2013-02, Vol.44 (2), p.715-723 |
| issn | 0939-4451 1438-2199 |
| language | eng |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Alytes obstetricans Amino Acid Sequence Amphibia Analytical Chemistry Animals Antimicrobial Cationic Peptides - chemical synthesis Antimicrobial Cationic Peptides - chemistry Antimicrobial Cationic Peptides - pharmacology Antineoplastic Agents - chemical synthesis Antineoplastic Agents - chemistry Antineoplastic Agents - pharmacology Anura Anura - metabolism Biochemical Engineering Biochemistry Biomedical and Life Sciences Cell Line, Tumor HT29 Cells Humans Life Sciences Molecular Sequence Data Neoplasms - drug therapy Neurobiology Original Article Proteomics Skin - chemistry Skin - metabolism Structure-Activity Relationship |
| title | Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent |
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