Bis-Lactam Peptide [<i>i</i>, <i>i</i>+4]-Stapling with α-Methylated Thialysines
Four bis-lactam [<i>i</i>, <i>i</i>+4]-stapled peptides with <span style="font-variant: small-caps;">d</span>- or <span style="font-variant: small-caps;">l</span>-α-methyl-thialysines were constructed on a model peptide sequence der...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-10-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/25/19/4506 |
| _version_ | 1797552010109648896 |
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| author | Bo Wu Weiping Zheng |
| author_facet | Bo Wu Weiping Zheng |
| author_sort | Bo Wu |
| collection | DOAJ |
| description | Four bis-lactam [<i>i</i>, <i>i</i>+4]-stapled peptides with <span style="font-variant: small-caps;">d</span>- or <span style="font-variant: small-caps;">l</span>-α-methyl-thialysines were constructed on a model peptide sequence derived from p110α[E545K] and subjected to circular dichroism (CD) and proteolytic stability assessment, alongside the corresponding bis-lactam [<i>i</i>, <i>i</i>+4]-stapled peptide with <span style="font-variant: small-caps;">l</span>-thialysine. The % α-helicity values of these four stapled peptides were found to be largely comparable to each other yet greater than that of the stapled peptide with <span style="font-variant: small-caps;">l</span>-thialysine. An <span style="font-variant: small-caps;">l</span>-α-methyl-thialysine-stapled peptide built on a model peptide sequence derived from ribonuclease A (RNase A) was also found to exhibit a greater % α-helicity than its <span style="font-variant: small-caps;">l</span>-thialysine-stapled counterpart. Moreover, a greater proteolytic stability was demonstrated for the <span style="font-variant: small-caps;">l</span>-α-methyl-thialysine-stapled p110α[E545K] and RNase A peptides than that of their respective <span style="font-variant: small-caps;">l</span>-thialysine-stapled counterparts. |
| first_indexed | 2024-03-10T15:54:01Z |
| format | Article |
| id | doaj.art-864b18c86eef4a8c8b34032b9fe96efb |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T15:54:01Z |
| publishDate | 2020-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-864b18c86eef4a8c8b34032b9fe96efb2023-11-20T15:47:48ZengMDPI AGMolecules1420-30492020-10-012519450610.3390/molecules25194506Bis-Lactam Peptide [<i>i</i>, <i>i</i>+4]-Stapling with α-Methylated ThialysinesBo Wu0Weiping Zheng1School of Pharmacy, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, Jiangsu Province, ChinaSchool of Pharmacy, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, Jiangsu Province, ChinaFour bis-lactam [<i>i</i>, <i>i</i>+4]-stapled peptides with <span style="font-variant: small-caps;">d</span>- or <span style="font-variant: small-caps;">l</span>-α-methyl-thialysines were constructed on a model peptide sequence derived from p110α[E545K] and subjected to circular dichroism (CD) and proteolytic stability assessment, alongside the corresponding bis-lactam [<i>i</i>, <i>i</i>+4]-stapled peptide with <span style="font-variant: small-caps;">l</span>-thialysine. The % α-helicity values of these four stapled peptides were found to be largely comparable to each other yet greater than that of the stapled peptide with <span style="font-variant: small-caps;">l</span>-thialysine. An <span style="font-variant: small-caps;">l</span>-α-methyl-thialysine-stapled peptide built on a model peptide sequence derived from ribonuclease A (RNase A) was also found to exhibit a greater % α-helicity than its <span style="font-variant: small-caps;">l</span>-thialysine-stapled counterpart. Moreover, a greater proteolytic stability was demonstrated for the <span style="font-variant: small-caps;">l</span>-α-methyl-thialysine-stapled p110α[E545K] and RNase A peptides than that of their respective <span style="font-variant: small-caps;">l</span>-thialysine-stapled counterparts.https://www.mdpi.com/1420-3049/25/19/4506peptide staplingbis-lactam [<i>i</i>, <i>i</i>+4]-staplingα-methyl-thialysine% α-helicityproteolytic stability |
| spellingShingle | Bo Wu Weiping Zheng Bis-Lactam Peptide [<i>i</i>, <i>i</i>+4]-Stapling with α-Methylated Thialysines Molecules peptide stapling bis-lactam [<i>i</i>, <i>i</i>+4]-stapling α-methyl-thialysine % α-helicity proteolytic stability |
| title | Bis-Lactam Peptide [<i>i</i>, <i>i</i>+4]-Stapling with α-Methylated Thialysines |
| title_full | Bis-Lactam Peptide [<i>i</i>, <i>i</i>+4]-Stapling with α-Methylated Thialysines |
| title_fullStr | Bis-Lactam Peptide [<i>i</i>, <i>i</i>+4]-Stapling with α-Methylated Thialysines |
| title_full_unstemmed | Bis-Lactam Peptide [<i>i</i>, <i>i</i>+4]-Stapling with α-Methylated Thialysines |
| title_short | Bis-Lactam Peptide [<i>i</i>, <i>i</i>+4]-Stapling with α-Methylated Thialysines |
| title_sort | bis lactam peptide i i i i i i 4 stapling with α methylated thialysines |
| topic | peptide stapling bis-lactam [<i>i</i>, <i>i</i>+4]-stapling α-methyl-thialysine % α-helicity proteolytic stability |
| url | https://www.mdpi.com/1420-3049/25/19/4506 |
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