Table 1 Overview of the amyloid-like APR crystal structures

From: Polymorphic amyloid nanostructures of hormone peptides involved in glucose homeostasis display reversible amyloid formation

APR

Polymorph

PDB ID

Crystallization conditions

Backbone conformer(s)a

Co-crystallising reagent(s)

Amyloid classb

Shifted assembly modec

DFINWL

(GLP-2)

A

8ANJ

70% H2O / 30% ACN, 0.1% TFA, 37 °C

at acidic conditions (pH: 2–3)

A1 (skyblue)

H2O

class 1

parallel

Slight lateral shift

between every

second sheet

pEFIAWL

(GLP-1)

A

8ANK

70% H2O / 30% ACN, 0.1% TFA, 37 °C

at acidic conditions (pH: 2–3)

A1 (deepsalmon)

H2O

class 7

antiparallel

No shift

Ac-EFIAWL

(GLP-1)

A

8ONQ

0.1 M citrate buffer, (pH: 4.0)

A1 (aquamarine)

A2 (deepblue)

H2O

class 7

antiparallel

Lateral shift between sheets

LFIEWL

(exendin-4)

A

8ANN

70% H2O / 30% ACN, 0.1% TFA, 37 °C

at acidic conditions (pH: 2–3)

A1 (greencyan)

H2O

class 8

antiparallel

No shift

B

8ANL

H2O, 37 °C, pH: 5.5

B1 (green)

B2 (limon)

B3 (darkyellow)

B4 (forestgreen)

H2O

class 7 / 8

antiparallel

Lateral shift

between sheets

LYIQWL

(Tc5b, E19)

A

8ANH

66% H2O / 33% ACN, 0,1% TFA, 4 °C,

at acidic conditions (pH: 2–3)

A1 (lightpurple)

A2 (deeppurple)

H2O, ACN, TFA

class 8

antiparallel

Shifted along

the β-spine axis

B

8ANM

H2O, 37 °C, at isoelectric point

of the peptide (pH: 5.6)

B1 (teal)

H2O

class 8

antiparallel

Lateral shift

between sheets

C

8ANI

90% H2O / 10% EtOH, 37 °C

at acidic conditions (pH: 3–5)

C1 (orange)

C2 (olive)

H2O, EtOH, TFA

class 8

antiparallel

Shifted along

the β-spine axis

D

8ANG

70% H2O / 30% EtOH, 37 °C, at acidic

or neutral conditions (pH: 4–7)

D1 (red)

EtOH

class 1 / 4

parallel

Lateral shift

between sheets

  1. aAccording to Fig. 4.
  2. bAmyloid classes are defined based on Eisenberg classification32.
  3. cAdjacent β-sheets may shift perpendicular to the fibril axis, showing laterally displaced contacting surfaces. β-strand dimers can displace along the β-spine axis, disrupting its axial continuality.