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Review Article

Cyclotides: a natural combinatorial peptide library or a bioactive sequence player?

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Pages 575-580 | Received 04 Aug 2014, Accepted 09 Aug 2014, Published online: 22 Sep 2014

Figures & data

Figure 1. Pymol generated view of the uterotonic polypeptide kalata B1structure characterized by three disulphide bonds.

Figure 1. Pymol generated view of the uterotonic polypeptide kalata B1structure characterized by three disulphide bonds.

Figure 2. Sequences of significative cyclotides belong to the two subfamilies Möebius type and Bracelet type.

Figure 2. Sequences of significative cyclotides belong to the two subfamilies Möebius type and Bracelet type.

Figure 3. Cyclotides’ synthetic strategy based on the random oxidation of deprotected cysteines.

Figure 3. Cyclotides’ synthetic strategy based on the random oxidation of deprotected cysteines.

Scheme 1. Schematic representation of the double use of cyclotides; on the right: natural sources of bioactive compounds; on the left: scaffold engineered bearing an external bioactive peptide sequence.

Scheme 1. Schematic representation of the double use of cyclotides; on the right: natural sources of bioactive compounds; on the left: scaffold engineered bearing an external bioactive peptide sequence.

Table 1. Kalata B7 and loop 3 fragment analogues with oxytocic and vasopressin like activityCitation20.

Figure 4. Bioactive peptide (new sequence) grafting in place of the native loop 6 of cyclotide scaffold.

Figure 4. Bioactive peptide (new sequence) grafting in place of the native loop 6 of cyclotide scaffold.

Table 2. Part ACitation26: two relevant requences used for grafting in place of loop 6 with bradychinin activity. Part BCitation27: four sequences used for grafting in place of loop 6 of Kalata B1 with MCR activity.

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