Solid phase synthesis and conformation of sequential glycosylated polytripeptide sequences related to antifreeze glycoproteins

Filira, Fernando; Biondi, Laura; Scolaro, Barbara; Foffani, M. T.; Mammi, Stefano; Peggion, Evaristo; Rocchi, Raniero

doi:10.1016/0141-8130(90)90080-t

Cited by 47 publications

(23 citation statements)

References 40 publications

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“…As a result, there have been many reports of synthetically modified AFGPs. These analogs are easier to synthesize than native AFGPs and often have modifications where the native disaccharide moiety, the polypeptide backbone, and the nature of the glycosidic linkage between the carbohydrate and polypeptide backbone have been simplified. Ben et al were the first to study the importance of the glycosidic linkage using C ‐linked AFGP analogs .…”

Section: Alternatives To Natural Af(g)psmentioning

confidence: 99%

Designing the next generation of cryoprotectants – From proteins to small molecules

et al. 2018

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During the past decade, there have been many exciting advances in the fields of cellular therapies, regenerative medicine, and tissue engineering. However, current cryopreservation strategies and protocols result in inferior product after thawing. Thus, novel cryoprotectants and protocols capable of meeting the high‐quality product(s) necessary for these therapies are urgently required. The search for new and improved cryoprotectants has been ongoing but novel small molecule ice recrystallization inhibitors, originally developed from naturally occurring antifreeze proteins, have demonstrated tremendous promise and will play a significant role in fully translating cellular and regenerative therapies into the clinical environment.

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Section: Alternatives To Natural Af(g)psmentioning

confidence: 99%

Designing the next generation of cryoprotectants – From proteins to small molecules

et al. 2018

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“…Related solid phase synthesis procedures for AFGPs containing single sugars were reported by Filira et al and Meldal and Jensen [72,77] by employing continuous flow solid-phase techniques or a stepwise elongation of the peptide backbone using a glycoconjugate (Figure 5B). The advantage of solid-phase synthesis over the solution phase route is the ability to synthesis diverse AFGP analogues by varying the length, sequence, nature of amino acid residues, and carbohydrate moieties using the Fmoc-protected building block.…”

Section: Synthesis Of Afgp Analoguesmentioning

confidence: 99%

“…The advantage of solid-phase synthesis over the solution phase route is the ability to synthesis diverse AFGP analogues by varying the length, sequence, nature of amino acid residues, and carbohydrate moieties using the Fmoc-protected building block. In addition, this route avoids the tedious purification of a mixture of oligomers and does not require a single tripeptide unit for the polymerization reaction [72,77]. The report by Filira et al .…”

Section: Synthesis Of Afgp Analoguesmentioning

confidence: 99%

“…The report by Filira et al . [72] was the first attempt to demonstrate the utility of solid-phase synthesis for the preparation of range of glycopeptides with lengths varying between 6 and 21 residues using N -α-(fluoren-9-ylmethoxycarbonyl)-3- O -(2,3,4,6-tetra- O -acetyl-α- d -galactopyranosyl)- l -threonine as a symmetrical anhydride [72]. Similarly, Meldal et al [77] synthesized AFGP analogues lacking the terminal galactose and the N -acetyl group, and with a substitution of the threonine residue in the alanyl-threonyl-alanyl (Ala-Thr-Ala) polypeptide with serine.…”

Section: Synthesis Of Afgp Analoguesmentioning

confidence: 99%

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Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology

et al. 2013

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Antifreeze proteins (AFPs) and glycoproteins (AFGPs), collectively called AF(G)Ps, constitute a diverse class of proteins found in various Arctic and Antarctic fish, as well as in amphibians, plants, and insects. These compounds possess the ability to inhibit the formation of ice and are therefore essential to the survival of many marine teleost fishes that routinely encounter sub-zero temperatures. Owing to this property, AF(G)Ps have potential applications in many areas such as storage of cells or tissues at low temperature, ice slurries for refrigeration systems, and food storage. In contrast to AFGPs, which are composed of repeated tripeptide units (Ala-Ala-Thr)n with minor sequence variations, AFPs possess very different primary, secondary, and tertiary structures. The isolation and purification of AFGPs is laborious, costly, and often results in mixtures, making characterization difficult. Recent structural investigations into the mechanism by which linear and cyclic AFGPs inhibit ice crystallization have led to significant progress toward the synthesis and assessment of several synthetic mimics of AFGPs. This review article will summarize synthetic AFGP mimics as well as current challenges in designing compounds capable of mimicking AFGPs. It will also cover our recent efforts in exploring whether peptoid mimics can serve as structural and functional mimics of native AFGPs.

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“…The glycosylation of serine and threonine in the trans ‐Gölgi apparatus plays an important, yet poorly defined, role in the metabolism of many glycoproteins, particularly in transport phenomena (18), intercellular recognition (19–21) and resistance to enzymatic degradation (22). A handful of studies focused on the intrinsic helical nature of glycosylated amino acids (23–26). Some of these pioneering studies suggested that glycosylation of amino acid residues disrupts helicity.…”

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confidence: 99%

O‐Linked glycopeptides retain helicity in water

Palian

Jacobsen

Polt

2001

The Journal of Peptide Research

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A 17-residue O-linked glycopeptide model incorporating a central alpha-mannosyl serine residue, and its unglycosylated analog both demonstrate substantial helicity in water. The peptide sequence was derived from previous studies in which differences in overall helicity as a function of single amino acid substitutions were measured by circular dichroism (CD). The helical content was predicted by molecular modeling, and confirmed by CD and NMR. Moreover, the glycopeptide retained its helicity in the presence of SDS micelles, whereas the native peptide lost secondary structure in the presence of micelles. The inference is that the peptide sequence is a more important helix determinant than glycosylation per se.

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Solid phase synthesis and conformation of sequential glycosylated polytripeptide sequences related to antifreeze glycoproteins

Cited by 47 publications

References 40 publications

Designing the next generation of cryoprotectants – From proteins to small molecules

Designing the next generation of cryoprotectants – From proteins to small molecules

Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology

O‐Linked glycopeptides retain helicity in water

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